t denticola atcc 35405  (ATCC)


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    Name:
    Treponema denticola
    Description:

    Catalog Number:
    35405
    Price:
    None
    Applications:
    Produces major surface proteinProduces methyl-accepting chemotaxis proteinProduces prolyl aminopeptidase proline iminopeptidase
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    Structured Review

    ATCC t denticola atcc 35405
    Interactions of rMsp antibodies with T. <t>denticola</t> <t>ATCC</t> 35405 cells and of whole-cell antibodies with rMsp fragments. (Panel A) Reactivity in ELISA of antiserum (1:250 diluted) to T. denticola ATCC 35405 cells (W) or antisera (1:250 diluted) raised to

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    Images

    1) Product Images from "Binding Properties and Adhesion-Mediating Regions of the Major Sheath Protein of Treponema denticola ATCC 35405"

    Article Title: Binding Properties and Adhesion-Mediating Regions of the Major Sheath Protein of Treponema denticola ATCC 35405

    Journal: Infection and Immunity

    doi: 10.1128/IAI.73.5.2891-2898.2005

    Interactions of rMsp antibodies with T. denticola ATCC 35405 cells and of whole-cell antibodies with rMsp fragments. (Panel A) Reactivity in ELISA of antiserum (1:250 diluted) to T. denticola ATCC 35405 cells (W) or antisera (1:250 diluted) raised to
    Figure Legend Snippet: Interactions of rMsp antibodies with T. denticola ATCC 35405 cells and of whole-cell antibodies with rMsp fragments. (Panel A) Reactivity in ELISA of antiserum (1:250 diluted) to T. denticola ATCC 35405 cells (W) or antisera (1:250 diluted) raised to

    Techniques Used: Enzyme-linked Immunosorbent Assay

    Reactivities of Msp antisera with T. denticola ATCC 35405 outer membrane protein extracts. (Panel A) SDS-PAGE gel of outer membrane proteins. (Panel B) Western blots reacted with antisera to rN-Msp (lane 1), rV-Msp (lane 2), or rC-Msp (lane 3). Molecular
    Figure Legend Snippet: Reactivities of Msp antisera with T. denticola ATCC 35405 outer membrane protein extracts. (Panel A) SDS-PAGE gel of outer membrane proteins. (Panel B) Western blots reacted with antisera to rN-Msp (lane 1), rV-Msp (lane 2), or rC-Msp (lane 3). Molecular

    Techniques Used: SDS Page, Western Blot

    Binding of rMsp to human fibronectin and to 30-kDa N-terminal fragment of human fibronectin. (Panel A) Western blot overlay of trypsin-derived fragments of human plasma fibronectin reacted with rMsp (lane 1) or with biotinylated T. denticola ATCC 35405
    Figure Legend Snippet: Binding of rMsp to human fibronectin and to 30-kDa N-terminal fragment of human fibronectin. (Panel A) Western blot overlay of trypsin-derived fragments of human plasma fibronectin reacted with rMsp (lane 1) or with biotinylated T. denticola ATCC 35405

    Techniques Used: Binding Assay, Western Blot, Derivative Assay

    Diagrammatic representation of the Msp sequences from T. denticola ATCC 35520 (A), strain ATCC 35405 (B), and of recombinant Msp polypeptides rMsp (530 aa residues), rN-Msp (189 aa residues), rV-Msp (57 aa residues), and rN-Msp (272 aa residues), with
    Figure Legend Snippet: Diagrammatic representation of the Msp sequences from T. denticola ATCC 35520 (A), strain ATCC 35405 (B), and of recombinant Msp polypeptides rMsp (530 aa residues), rN-Msp (189 aa residues), rV-Msp (57 aa residues), and rN-Msp (272 aa residues), with

    Techniques Used: Recombinant

    Effect of exogenously added rMsp on adhesion of Treponema strains to immobilized human fibronectin or 30-kDa fibronectin fragment. (Panel A) Adhesion levels of T. denticola ATCC 35405 cells to 0.1 μg fibronectin (filled column) or 30-kDa fibronectin
    Figure Legend Snippet: Effect of exogenously added rMsp on adhesion of Treponema strains to immobilized human fibronectin or 30-kDa fibronectin fragment. (Panel A) Adhesion levels of T. denticola ATCC 35405 cells to 0.1 μg fibronectin (filled column) or 30-kDa fibronectin

    Techniques Used:

    2) Product Images from "Binding Properties and Adhesion-Mediating Regions of the Major Sheath Protein of Treponema denticola ATCC 35405"

    Article Title: Binding Properties and Adhesion-Mediating Regions of the Major Sheath Protein of Treponema denticola ATCC 35405

    Journal: Infection and Immunity

    doi: 10.1128/IAI.73.5.2891-2898.2005

    Interactions of rMsp antibodies with T. denticola ATCC 35405 cells and of whole-cell antibodies with rMsp fragments. (Panel A) Reactivity in ELISA of antiserum (1:250 diluted) to T. denticola ATCC 35405 cells (W) or antisera (1:250 diluted) raised to
    Figure Legend Snippet: Interactions of rMsp antibodies with T. denticola ATCC 35405 cells and of whole-cell antibodies with rMsp fragments. (Panel A) Reactivity in ELISA of antiserum (1:250 diluted) to T. denticola ATCC 35405 cells (W) or antisera (1:250 diluted) raised to

    Techniques Used: Enzyme-linked Immunosorbent Assay

    Reactivities of Msp antisera with T. denticola ATCC 35405 outer membrane protein extracts. (Panel A) SDS-PAGE gel of outer membrane proteins. (Panel B) Western blots reacted with antisera to rN-Msp (lane 1), rV-Msp (lane 2), or rC-Msp (lane 3). Molecular
    Figure Legend Snippet: Reactivities of Msp antisera with T. denticola ATCC 35405 outer membrane protein extracts. (Panel A) SDS-PAGE gel of outer membrane proteins. (Panel B) Western blots reacted with antisera to rN-Msp (lane 1), rV-Msp (lane 2), or rC-Msp (lane 3). Molecular

    Techniques Used: SDS Page, Western Blot

    Binding of rMsp to human fibronectin and to 30-kDa N-terminal fragment of human fibronectin. (Panel A) Western blot overlay of trypsin-derived fragments of human plasma fibronectin reacted with rMsp (lane 1) or with biotinylated T. denticola ATCC 35405
    Figure Legend Snippet: Binding of rMsp to human fibronectin and to 30-kDa N-terminal fragment of human fibronectin. (Panel A) Western blot overlay of trypsin-derived fragments of human plasma fibronectin reacted with rMsp (lane 1) or with biotinylated T. denticola ATCC 35405

    Techniques Used: Binding Assay, Western Blot, Derivative Assay

    Diagrammatic representation of the Msp sequences from T. denticola ATCC 35520 (A), strain ATCC 35405 (B), and of recombinant Msp polypeptides rMsp (530 aa residues), rN-Msp (189 aa residues), rV-Msp (57 aa residues), and rN-Msp (272 aa residues), with
    Figure Legend Snippet: Diagrammatic representation of the Msp sequences from T. denticola ATCC 35520 (A), strain ATCC 35405 (B), and of recombinant Msp polypeptides rMsp (530 aa residues), rN-Msp (189 aa residues), rV-Msp (57 aa residues), and rN-Msp (272 aa residues), with

    Techniques Used: Recombinant

    Effect of exogenously added rMsp on adhesion of Treponema strains to immobilized human fibronectin or 30-kDa fibronectin fragment. (Panel A) Adhesion levels of T. denticola ATCC 35405 cells to 0.1 μg fibronectin (filled column) or 30-kDa fibronectin
    Figure Legend Snippet: Effect of exogenously added rMsp on adhesion of Treponema strains to immobilized human fibronectin or 30-kDa fibronectin fragment. (Panel A) Adhesion levels of T. denticola ATCC 35405 cells to 0.1 μg fibronectin (filled column) or 30-kDa fibronectin

    Techniques Used:

    3) Product Images from "Binding Properties and Adhesion-Mediating Regions of the Major Sheath Protein of Treponema denticola ATCC 35405"

    Article Title: Binding Properties and Adhesion-Mediating Regions of the Major Sheath Protein of Treponema denticola ATCC 35405

    Journal: Infection and Immunity

    doi: 10.1128/IAI.73.5.2891-2898.2005

    Interactions of rMsp antibodies with T. denticola ATCC 35405 cells and of whole-cell antibodies with rMsp fragments. (Panel A) Reactivity in ELISA of antiserum (1:250 diluted) to T. denticola ATCC 35405 cells (W) or antisera (1:250 diluted) raised to
    Figure Legend Snippet: Interactions of rMsp antibodies with T. denticola ATCC 35405 cells and of whole-cell antibodies with rMsp fragments. (Panel A) Reactivity in ELISA of antiserum (1:250 diluted) to T. denticola ATCC 35405 cells (W) or antisera (1:250 diluted) raised to

    Techniques Used: Enzyme-linked Immunosorbent Assay

    Reactivities of Msp antisera with T. denticola ATCC 35405 outer membrane protein extracts. (Panel A) SDS-PAGE gel of outer membrane proteins. (Panel B) Western blots reacted with antisera to rN-Msp (lane 1), rV-Msp (lane 2), or rC-Msp (lane 3). Molecular
    Figure Legend Snippet: Reactivities of Msp antisera with T. denticola ATCC 35405 outer membrane protein extracts. (Panel A) SDS-PAGE gel of outer membrane proteins. (Panel B) Western blots reacted with antisera to rN-Msp (lane 1), rV-Msp (lane 2), or rC-Msp (lane 3). Molecular

    Techniques Used: SDS Page, Western Blot

    Binding of rMsp to human fibronectin and to 30-kDa N-terminal fragment of human fibronectin. (Panel A) Western blot overlay of trypsin-derived fragments of human plasma fibronectin reacted with rMsp (lane 1) or with biotinylated T. denticola ATCC 35405
    Figure Legend Snippet: Binding of rMsp to human fibronectin and to 30-kDa N-terminal fragment of human fibronectin. (Panel A) Western blot overlay of trypsin-derived fragments of human plasma fibronectin reacted with rMsp (lane 1) or with biotinylated T. denticola ATCC 35405

    Techniques Used: Binding Assay, Western Blot, Derivative Assay

    Diagrammatic representation of the Msp sequences from T. denticola ATCC 35520 (A), strain ATCC 35405 (B), and of recombinant Msp polypeptides rMsp (530 aa residues), rN-Msp (189 aa residues), rV-Msp (57 aa residues), and rN-Msp (272 aa residues), with
    Figure Legend Snippet: Diagrammatic representation of the Msp sequences from T. denticola ATCC 35520 (A), strain ATCC 35405 (B), and of recombinant Msp polypeptides rMsp (530 aa residues), rN-Msp (189 aa residues), rV-Msp (57 aa residues), and rN-Msp (272 aa residues), with

    Techniques Used: Recombinant

    Effect of exogenously added rMsp on adhesion of Treponema strains to immobilized human fibronectin or 30-kDa fibronectin fragment. (Panel A) Adhesion levels of T. denticola ATCC 35405 cells to 0.1 μg fibronectin (filled column) or 30-kDa fibronectin
    Figure Legend Snippet: Effect of exogenously added rMsp on adhesion of Treponema strains to immobilized human fibronectin or 30-kDa fibronectin fragment. (Panel A) Adhesion levels of T. denticola ATCC 35405 cells to 0.1 μg fibronectin (filled column) or 30-kDa fibronectin

    Techniques Used:

    4) Product Images from "Genome-Wide Relatedness of Treponema pedis, from Gingiva and Necrotic Skin Lesions of Pigs, with the Human Oral Pathogen Treponema denticola"

    Article Title: Genome-Wide Relatedness of Treponema pedis, from Gingiva and Necrotic Skin Lesions of Pigs, with the Human Oral Pathogen Treponema denticola

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0071281

    Circular representation of the T. pedis T A4 genome and complete genome alignment with T. denticola . (A.) Circular representation of the T. pedis T A4 genome. The CDSs are shown in violet where the outer circle represents predictions on the plus strand and the second circle those on the minus strand. CDSs with a best BLASTP hit in T. denticola ATCC 35405 are colored red and shown in the third circle. The fourth circle represents genes with best BLASTP hits in T. brennaborense (black), F. nucleatum (green), F. alocis (blue) and T. succinifaciens (grey). G+C skew is drawn in the inner circle. (B.) Complete genome alignment between T. pedis T A4 and T. denticola ATCC 35405. Dots represent maximum unique matches (MUMs) between the genomes. MUMs oriented in the same direction are depicted as red dots and reverse complemented MUMs are depicted as blue dots.
    Figure Legend Snippet: Circular representation of the T. pedis T A4 genome and complete genome alignment with T. denticola . (A.) Circular representation of the T. pedis T A4 genome. The CDSs are shown in violet where the outer circle represents predictions on the plus strand and the second circle those on the minus strand. CDSs with a best BLASTP hit in T. denticola ATCC 35405 are colored red and shown in the third circle. The fourth circle represents genes with best BLASTP hits in T. brennaborense (black), F. nucleatum (green), F. alocis (blue) and T. succinifaciens (grey). G+C skew is drawn in the inner circle. (B.) Complete genome alignment between T. pedis T A4 and T. denticola ATCC 35405. Dots represent maximum unique matches (MUMs) between the genomes. MUMs oriented in the same direction are depicted as red dots and reverse complemented MUMs are depicted as blue dots.

    Techniques Used:

    5) Product Images from "Genome-Wide Relatedness of Treponema pedis, from Gingiva and Necrotic Skin Lesions of Pigs, with the Human Oral Pathogen Treponema denticola"

    Article Title: Genome-Wide Relatedness of Treponema pedis, from Gingiva and Necrotic Skin Lesions of Pigs, with the Human Oral Pathogen Treponema denticola

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0071281

    Circular representation of the T. pedis T A4 genome and complete genome alignment with T. denticola . (A.) Circular representation of the T. pedis T A4 genome. The CDSs are shown in violet where the outer circle represents predictions on the plus strand and the second circle those on the minus strand. CDSs with a best BLASTP hit in T. denticola ATCC 35405 are colored red and shown in the third circle. The fourth circle represents genes with best BLASTP hits in T. brennaborense (black), F. nucleatum (green), F. alocis (blue) and T. succinifaciens (grey). G+C skew is drawn in the inner circle. (B.) Complete genome alignment between T. pedis T A4 and T. denticola ATCC 35405. Dots represent maximum unique matches (MUMs) between the genomes. MUMs oriented in the same direction are depicted as red dots and reverse complemented MUMs are depicted as blue dots.
    Figure Legend Snippet: Circular representation of the T. pedis T A4 genome and complete genome alignment with T. denticola . (A.) Circular representation of the T. pedis T A4 genome. The CDSs are shown in violet where the outer circle represents predictions on the plus strand and the second circle those on the minus strand. CDSs with a best BLASTP hit in T. denticola ATCC 35405 are colored red and shown in the third circle. The fourth circle represents genes with best BLASTP hits in T. brennaborense (black), F. nucleatum (green), F. alocis (blue) and T. succinifaciens (grey). G+C skew is drawn in the inner circle. (B.) Complete genome alignment between T. pedis T A4 and T. denticola ATCC 35405. Dots represent maximum unique matches (MUMs) between the genomes. MUMs oriented in the same direction are depicted as red dots and reverse complemented MUMs are depicted as blue dots.

    Techniques Used:

    6) Product Images from "Genome-Wide Relatedness of Treponema pedis, from Gingiva and Necrotic Skin Lesions of Pigs, with the Human Oral Pathogen Treponema denticola"

    Article Title: Genome-Wide Relatedness of Treponema pedis, from Gingiva and Necrotic Skin Lesions of Pigs, with the Human Oral Pathogen Treponema denticola

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0071281

    Circular representation of the T. pedis T A4 genome and complete genome alignment with T. denticola . (A.) Circular representation of the T. pedis T A4 genome. The CDSs are shown in violet where the outer circle represents predictions on the plus strand and the second circle those on the minus strand. CDSs with a best BLASTP hit in T. denticola ATCC 35405 are colored red and shown in the third circle. The fourth circle represents genes with best BLASTP hits in T. brennaborense (black), F. nucleatum (green), F. alocis (blue) and T. succinifaciens (grey). G+C skew is drawn in the inner circle. (B.) Complete genome alignment between T. pedis T A4 and T. denticola ATCC 35405. Dots represent maximum unique matches (MUMs) between the genomes. MUMs oriented in the same direction are depicted as red dots and reverse complemented MUMs are depicted as blue dots.
    Figure Legend Snippet: Circular representation of the T. pedis T A4 genome and complete genome alignment with T. denticola . (A.) Circular representation of the T. pedis T A4 genome. The CDSs are shown in violet where the outer circle represents predictions on the plus strand and the second circle those on the minus strand. CDSs with a best BLASTP hit in T. denticola ATCC 35405 are colored red and shown in the third circle. The fourth circle represents genes with best BLASTP hits in T. brennaborense (black), F. nucleatum (green), F. alocis (blue) and T. succinifaciens (grey). G+C skew is drawn in the inner circle. (B.) Complete genome alignment between T. pedis T A4 and T. denticola ATCC 35405. Dots represent maximum unique matches (MUMs) between the genomes. MUMs oriented in the same direction are depicted as red dots and reverse complemented MUMs are depicted as blue dots.

    Techniques Used:

    7) Product Images from "Genome-Wide Relatedness of Treponema pedis, from Gingiva and Necrotic Skin Lesions of Pigs, with the Human Oral Pathogen Treponema denticola"

    Article Title: Genome-Wide Relatedness of Treponema pedis, from Gingiva and Necrotic Skin Lesions of Pigs, with the Human Oral Pathogen Treponema denticola

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0071281

    Circular representation of the T. pedis T A4 genome and complete genome alignment with T. denticola . (A.) Circular representation of the T. pedis T A4 genome. The CDSs are shown in violet where the outer circle represents predictions on the plus strand and the second circle those on the minus strand. CDSs with a best BLASTP hit in T. denticola ATCC 35405 are colored red and shown in the third circle. The fourth circle represents genes with best BLASTP hits in T. brennaborense (black), F. nucleatum (green), F. alocis (blue) and T. succinifaciens (grey). G+C skew is drawn in the inner circle. (B.) Complete genome alignment between T. pedis T A4 and T. denticola ATCC 35405. Dots represent maximum unique matches (MUMs) between the genomes. MUMs oriented in the same direction are depicted as red dots and reverse complemented MUMs are depicted as blue dots.
    Figure Legend Snippet: Circular representation of the T. pedis T A4 genome and complete genome alignment with T. denticola . (A.) Circular representation of the T. pedis T A4 genome. The CDSs are shown in violet where the outer circle represents predictions on the plus strand and the second circle those on the minus strand. CDSs with a best BLASTP hit in T. denticola ATCC 35405 are colored red and shown in the third circle. The fourth circle represents genes with best BLASTP hits in T. brennaborense (black), F. nucleatum (green), F. alocis (blue) and T. succinifaciens (grey). G+C skew is drawn in the inner circle. (B.) Complete genome alignment between T. pedis T A4 and T. denticola ATCC 35405. Dots represent maximum unique matches (MUMs) between the genomes. MUMs oriented in the same direction are depicted as red dots and reverse complemented MUMs are depicted as blue dots.

    Techniques Used:

    8) Product Images from "Motility and Chemotaxis in Tissue Penetration of Oral Epithelial Cell Layers by Treponema denticola"

    Article Title: Motility and Chemotaxis in Tissue Penetration of Oral Epithelial Cell Layers by Treponema denticola

    Journal: Infection and Immunity

    doi: 10.1128/IAI.69.10.6276-6283.2001

    Motility of wild-type T. denticola ATCC 35405 in KBM for epithelial cell lines in a 5% CO 2 atmosphere at 35°C (○) and under anaerobic conditions (85% N 2 , 10% H 2 , 5% CO 2 ) at 35°C (□). Values for each condition were obtained in triplicate in two independent experiments. More than 600 cells were examined for cellular motility in each experiment. All mutant derivatives except the nonmotile strain HL53 showed similar results (data not shown).
    Figure Legend Snippet: Motility of wild-type T. denticola ATCC 35405 in KBM for epithelial cell lines in a 5% CO 2 atmosphere at 35°C (○) and under anaerobic conditions (85% N 2 , 10% H 2 , 5% CO 2 ) at 35°C (□). Values for each condition were obtained in triplicate in two independent experiments. More than 600 cells were examined for cellular motility in each experiment. All mutant derivatives except the nonmotile strain HL53 showed similar results (data not shown).

    Techniques Used: Mutagenesis

    9) Product Images from "Composition and Localization of Treponema denticola Outer Membrane Complexes ▿"

    Article Title: Composition and Localization of Treponema denticola Outer Membrane Complexes ▿

    Journal: Infection and Immunity

    doi: 10.1128/IAI.05701-11

    Localization of T. denticola major surface protein and protease complex polypeptides. A surface localization immunofluorescence assay was performed with T. denticola ATCC 35405 with or without membrane permeabilization, using polyclonal antibodies raised
    Figure Legend Snippet: Localization of T. denticola major surface protein and protease complex polypeptides. A surface localization immunofluorescence assay was performed with T. denticola ATCC 35405 with or without membrane permeabilization, using polyclonal antibodies raised

    Techniques Used: Immunofluorescence

    10) Product Images from "A simplified erythromycin resistance cassette for Treponema denticola mutagenesis"

    Article Title: A simplified erythromycin resistance cassette for Treponema denticola mutagenesis

    Journal: Journal of microbiological methods

    doi: 10.1016/j.mimet.2010.07.020

    Construction of T. denticola mutants using ermF-ermB and ermB cassettes. The protease operon ( prcB-prcA-prtP ) and adjacent gene TDE0759 in wildtype parent strain ATCC 35405 and isogenic strains mutated in prcB (P0760 and CF548) and prcA (PNE and CF547) showing locations of ermF-ermB and ermB insertions. The symbol x- indicates gene disruption in prcA or prcB .
    Figure Legend Snippet: Construction of T. denticola mutants using ermF-ermB and ermB cassettes. The protease operon ( prcB-prcA-prtP ) and adjacent gene TDE0759 in wildtype parent strain ATCC 35405 and isogenic strains mutated in prcB (P0760 and CF548) and prcA (PNE and CF547) showing locations of ermF-ermB and ermB insertions. The symbol x- indicates gene disruption in prcA or prcB .

    Techniques Used:

    11) Product Images from "Dentilisin Activity Affects the Organization of the Outer Sheath of Treponema denticola"

    Article Title: Dentilisin Activity Affects the Organization of the Outer Sheath of Treponema denticola

    Journal: Journal of Bacteriology

    doi:

    Mean areas of lesions at infection sites after challenge with T. denticola ATCC 35405 and prtP mutant K1. Mice were injected with live T. denticola ATCC 35405 (open bars) or mutant K1 (hatched bars), and lesion areas were determined at the indicated times following infection.
    Figure Legend Snippet: Mean areas of lesions at infection sites after challenge with T. denticola ATCC 35405 and prtP mutant K1. Mice were injected with live T. denticola ATCC 35405 (open bars) or mutant K1 (hatched bars), and lesion areas were determined at the indicated times following infection.

    Techniques Used: Infection, Mutagenesis, Mouse Assay, Injection

    Immunoblot analysis of T. denticola ATCC 35405 and K1 with anti- T. denticola ATCC 35405 whole-cell serum. Samples from lanes 1 to 4 were treated with PMSF. Lanes 1 and 5, T. denticola ATCC 35405 (without boiling); lanes 2 and 6, T. denticola K1 (without boiling); lanes 3 and 7, T. denticola ATCC 35405 (with boiling); lanes 4 and 8, T. denticola K1 (with boiling). Arrowheads indicate the high-molecular-mass oligomeric protein and the Msp band.
    Figure Legend Snippet: Immunoblot analysis of T. denticola ATCC 35405 and K1 with anti- T. denticola ATCC 35405 whole-cell serum. Samples from lanes 1 to 4 were treated with PMSF. Lanes 1 and 5, T. denticola ATCC 35405 (without boiling); lanes 2 and 6, T. denticola K1 (without boiling); lanes 3 and 7, T. denticola ATCC 35405 (with boiling); lanes 4 and 8, T. denticola K1 (with boiling). Arrowheads indicate the high-molecular-mass oligomeric protein and the Msp band.

    Techniques Used:

    Southern blot analysis of T. denticola ATCC 35405 and prtP mutant K1. Chromosomal DNAs from T. denticola ATCC 35405 (lanes 1 and 3) and prtP mutant K1 (lanes 2 and 4) were digested with Hin dIII and hybridized with a digoxigenin-labeled Kpn I- Pst I fragment from the prtP gene (lanes 1 and 2) or the Kpn I- Bam HI fragment from pVA2198 (lanes 3 and 4). Numbers at right are kilobase pairs.
    Figure Legend Snippet: Southern blot analysis of T. denticola ATCC 35405 and prtP mutant K1. Chromosomal DNAs from T. denticola ATCC 35405 (lanes 1 and 3) and prtP mutant K1 (lanes 2 and 4) were digested with Hin dIII and hybridized with a digoxigenin-labeled Kpn I- Pst I fragment from the prtP gene (lanes 1 and 2) or the Kpn I- Bam HI fragment from pVA2198 (lanes 3 and 4). Numbers at right are kilobase pairs.

    Techniques Used: Southern Blot, Mutagenesis, Labeling

    Gelatin zymography of sonicates of T. denticola ATCC 35405 (lane 1) and K1 (lane 2).
    Figure Legend Snippet: Gelatin zymography of sonicates of T. denticola ATCC 35405 (lane 1) and K1 (lane 2).

    Techniques Used: Zymography

    SDS-PAGE analysis of sonicates of T. denticola ATCC 35405 and K1. Samples from lanes 1 to 4 were treated with PMSF. Lanes 1 and 5, T. denticola ATCC 35405 (without boiling); lanes 2 and 6, T. denticola K1 (without boiling); lanes 3 and 7, T. denticola ATCC 35405 (with boiling); lanes 4 and 8, T. denticola K1 (with boiling). After electrophoresis, the gel was stained with Coomassie brilliant blue R-250. Arrowheads indicate the high-molecular-mass oligomeric protein and the Msp band.
    Figure Legend Snippet: SDS-PAGE analysis of sonicates of T. denticola ATCC 35405 and K1. Samples from lanes 1 to 4 were treated with PMSF. Lanes 1 and 5, T. denticola ATCC 35405 (without boiling); lanes 2 and 6, T. denticola K1 (without boiling); lanes 3 and 7, T. denticola ATCC 35405 (with boiling); lanes 4 and 8, T. denticola K1 (with boiling). After electrophoresis, the gel was stained with Coomassie brilliant blue R-250. Arrowheads indicate the high-molecular-mass oligomeric protein and the Msp band.

    Techniques Used: SDS Page, Electrophoresis, Staining

    Immunoblot analysis of T. denticola ATCC 35405 (lane 1; boiled) and K1 (lane 2; boiled) with antidentilisin serum.
    Figure Legend Snippet: Immunoblot analysis of T. denticola ATCC 35405 (lane 1; boiled) and K1 (lane 2; boiled) with antidentilisin serum.

    Techniques Used:

    12) Product Images from "The central region of the msp gene of Treponema denticola has sequence heterogeneity among clinical samples, obtained from patients with periodontitis"

    Article Title: The central region of the msp gene of Treponema denticola has sequence heterogeneity among clinical samples, obtained from patients with periodontitis

    Journal: BMC Infectious Diseases

    doi: 10.1186/1471-2334-10-345

    MSP amino acid sequence alignment of T. denticola strains ATCC 35405 and Group A (panel A), and ATCC 33520 and Group B (panel B) . The grey areas indicate single amino acid substitutions compared with ATCC 35405 (panel A) and ATCC 33520 (panel B).
    Figure Legend Snippet: MSP amino acid sequence alignment of T. denticola strains ATCC 35405 and Group A (panel A), and ATCC 33520 and Group B (panel B) . The grey areas indicate single amino acid substitutions compared with ATCC 35405 (panel A) and ATCC 33520 (panel B).

    Techniques Used: Sequencing

    Diversity of msp sequences . Sequence alignments of 17 central regions (from 600 to 900 nucleotides) from T. denticola positive clinical specimens. In panel A are shown the clinical samples of Group A. In panel B are shown the clinical samples of Group B. The upper line contains the sequence of T. denticola strain ATCC 35405 and ATCC 33520, respectively, in both panels. The grey areas indicate variations of single nucleotide positions compared with T. denticola ATCC 35405.
    Figure Legend Snippet: Diversity of msp sequences . Sequence alignments of 17 central regions (from 600 to 900 nucleotides) from T. denticola positive clinical specimens. In panel A are shown the clinical samples of Group A. In panel B are shown the clinical samples of Group B. The upper line contains the sequence of T. denticola strain ATCC 35405 and ATCC 33520, respectively, in both panels. The grey areas indicate variations of single nucleotide positions compared with T. denticola ATCC 35405.

    Techniques Used: Sequencing

    Evolutionary relationships of T. denticola msp gene, deduced from the sequences of 17 clinical samples, ATCC 35405, ATCC 33520, and OTK . The phylogenetic analysis was performed using the neighbor-joining method with MEGA 4 on aligned sequences from the msp complete cds sequence (bootstrap values > 75 are shown at nodes).
    Figure Legend Snippet: Evolutionary relationships of T. denticola msp gene, deduced from the sequences of 17 clinical samples, ATCC 35405, ATCC 33520, and OTK . The phylogenetic analysis was performed using the neighbor-joining method with MEGA 4 on aligned sequences from the msp complete cds sequence (bootstrap values > 75 are shown at nodes).

    Techniques Used: Sequencing

    Antigenicity plot of T. denticola strains ATCC 35405 (frame A), ATCC 33520 (frame B), and 2 representative specimens (B66, frame C; B23, frame D) . In each frame, the area of the plot that is surrounded by a continuous line represents the central region of MSP. The internal smaller area, surrounded by the dotted line, represents the portion that has the greatest difference in predicted antigenicity between specimens B66 and B23 and ATCC35405.
    Figure Legend Snippet: Antigenicity plot of T. denticola strains ATCC 35405 (frame A), ATCC 33520 (frame B), and 2 representative specimens (B66, frame C; B23, frame D) . In each frame, the area of the plot that is surrounded by a continuous line represents the central region of MSP. The internal smaller area, surrounded by the dotted line, represents the portion that has the greatest difference in predicted antigenicity between specimens B66 and B23 and ATCC35405.

    Techniques Used:

    13) Product Images from "Characterization of a potential ABC-type bacteriocin exporter protein from Treponema denticola"

    Article Title: Characterization of a potential ABC-type bacteriocin exporter protein from Treponema denticola

    Journal: BMC Oral Health

    doi: 10.1186/s12903-016-0243-7

    Southern blot analysis of tepA1 ( a ), tepA2 ( b ) , and tepA3 ( c ). Genomic DNA from T. denticola strains was digested with Hin dIII. 1: genomic DNA from ATCC 33520, 2: genomic DNA from ATCC 33521, genomic DNA from ATCC 35404, 4: genomic DNA from ATCC 35405, 5: genomic DNA from GM1
    Figure Legend Snippet: Southern blot analysis of tepA1 ( a ), tepA2 ( b ) , and tepA3 ( c ). Genomic DNA from T. denticola strains was digested with Hin dIII. 1: genomic DNA from ATCC 33520, 2: genomic DNA from ATCC 33521, genomic DNA from ATCC 35404, 4: genomic DNA from ATCC 35405, 5: genomic DNA from GM1

    Techniques Used: Southern Blot

    14) Product Images from "Characterization of a potential ABC-type bacteriocin exporter protein from Treponema denticola"

    Article Title: Characterization of a potential ABC-type bacteriocin exporter protein from Treponema denticola

    Journal: BMC Oral Health

    doi: 10.1186/s12903-016-0243-7

    Southern blot analysis of tepA1 ( a ), tepA2 ( b ) , and tepA3 ( c ). Genomic DNA from T. denticola strains was digested with Hin dIII. 1: genomic DNA from ATCC 33520, 2: genomic DNA from ATCC 33521, genomic DNA from ATCC 35404, 4: genomic DNA from ATCC 35405, 5: genomic DNA from GM1
    Figure Legend Snippet: Southern blot analysis of tepA1 ( a ), tepA2 ( b ) , and tepA3 ( c ). Genomic DNA from T. denticola strains was digested with Hin dIII. 1: genomic DNA from ATCC 33520, 2: genomic DNA from ATCC 33521, genomic DNA from ATCC 35404, 4: genomic DNA from ATCC 35405, 5: genomic DNA from GM1

    Techniques Used: Southern Blot

    15) Product Images from "Binding Properties and Adhesion-Mediating Regions of the Major Sheath Protein of Treponema denticola ATCC 35405"

    Article Title: Binding Properties and Adhesion-Mediating Regions of the Major Sheath Protein of Treponema denticola ATCC 35405

    Journal: Infection and Immunity

    doi: 10.1128/IAI.73.5.2891-2898.2005

    Interactions of rMsp antibodies with T. denticola ATCC 35405 cells and of whole-cell antibodies with rMsp fragments. (Panel A) Reactivity in ELISA of antiserum (1:250 diluted) to T. denticola ATCC 35405 cells (W) or antisera (1:250 diluted) raised to
    Figure Legend Snippet: Interactions of rMsp antibodies with T. denticola ATCC 35405 cells and of whole-cell antibodies with rMsp fragments. (Panel A) Reactivity in ELISA of antiserum (1:250 diluted) to T. denticola ATCC 35405 cells (W) or antisera (1:250 diluted) raised to

    Techniques Used: Enzyme-linked Immunosorbent Assay

    Reactivities of Msp antisera with T. denticola ATCC 35405 outer membrane protein extracts. (Panel A) SDS-PAGE gel of outer membrane proteins. (Panel B) Western blots reacted with antisera to rN-Msp (lane 1), rV-Msp (lane 2), or rC-Msp (lane 3). Molecular
    Figure Legend Snippet: Reactivities of Msp antisera with T. denticola ATCC 35405 outer membrane protein extracts. (Panel A) SDS-PAGE gel of outer membrane proteins. (Panel B) Western blots reacted with antisera to rN-Msp (lane 1), rV-Msp (lane 2), or rC-Msp (lane 3). Molecular

    Techniques Used: SDS Page, Western Blot

    Binding of rMsp to human fibronectin and to 30-kDa N-terminal fragment of human fibronectin. (Panel A) Western blot overlay of trypsin-derived fragments of human plasma fibronectin reacted with rMsp (lane 1) or with biotinylated T. denticola ATCC 35405
    Figure Legend Snippet: Binding of rMsp to human fibronectin and to 30-kDa N-terminal fragment of human fibronectin. (Panel A) Western blot overlay of trypsin-derived fragments of human plasma fibronectin reacted with rMsp (lane 1) or with biotinylated T. denticola ATCC 35405

    Techniques Used: Binding Assay, Western Blot, Derivative Assay

    Diagrammatic representation of the Msp sequences from T. denticola ATCC 35520 (A), strain ATCC 35405 (B), and of recombinant Msp polypeptides rMsp (530 aa residues), rN-Msp (189 aa residues), rV-Msp (57 aa residues), and rN-Msp (272 aa residues), with
    Figure Legend Snippet: Diagrammatic representation of the Msp sequences from T. denticola ATCC 35520 (A), strain ATCC 35405 (B), and of recombinant Msp polypeptides rMsp (530 aa residues), rN-Msp (189 aa residues), rV-Msp (57 aa residues), and rN-Msp (272 aa residues), with

    Techniques Used: Recombinant

    Effect of exogenously added rMsp on adhesion of Treponema strains to immobilized human fibronectin or 30-kDa fibronectin fragment. (Panel A) Adhesion levels of T. denticola ATCC 35405 cells to 0.1 μg fibronectin (filled column) or 30-kDa fibronectin
    Figure Legend Snippet: Effect of exogenously added rMsp on adhesion of Treponema strains to immobilized human fibronectin or 30-kDa fibronectin fragment. (Panel A) Adhesion levels of T. denticola ATCC 35405 cells to 0.1 μg fibronectin (filled column) or 30-kDa fibronectin

    Techniques Used:

    16) Product Images from "Genome-Wide Relatedness of Treponema pedis, from Gingiva and Necrotic Skin Lesions of Pigs, with the Human Oral Pathogen Treponema denticola"

    Article Title: Genome-Wide Relatedness of Treponema pedis, from Gingiva and Necrotic Skin Lesions of Pigs, with the Human Oral Pathogen Treponema denticola

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0071281

    Circular representation of the T. pedis T A4 genome and complete genome alignment with T. denticola . (A.) Circular representation of the T. pedis T A4 genome. The CDSs are shown in violet where the outer circle represents predictions on the plus strand and the second circle those on the minus strand. CDSs with a best BLASTP hit in T. denticola ATCC 35405 are colored red and shown in the third circle. The fourth circle represents genes with best BLASTP hits in T. brennaborense (black), F. nucleatum (green), F. alocis (blue) and T. succinifaciens (grey). G+C skew is drawn in the inner circle. (B.) Complete genome alignment between T. pedis T A4 and T. denticola ATCC 35405. Dots represent maximum unique matches (MUMs) between the genomes. MUMs oriented in the same direction are depicted as red dots and reverse complemented MUMs are depicted as blue dots.
    Figure Legend Snippet: Circular representation of the T. pedis T A4 genome and complete genome alignment with T. denticola . (A.) Circular representation of the T. pedis T A4 genome. The CDSs are shown in violet where the outer circle represents predictions on the plus strand and the second circle those on the minus strand. CDSs with a best BLASTP hit in T. denticola ATCC 35405 are colored red and shown in the third circle. The fourth circle represents genes with best BLASTP hits in T. brennaborense (black), F. nucleatum (green), F. alocis (blue) and T. succinifaciens (grey). G+C skew is drawn in the inner circle. (B.) Complete genome alignment between T. pedis T A4 and T. denticola ATCC 35405. Dots represent maximum unique matches (MUMs) between the genomes. MUMs oriented in the same direction are depicted as red dots and reverse complemented MUMs are depicted as blue dots.

    Techniques Used:

    17) Product Images from "Genome-Wide Relatedness of Treponema pedis, from Gingiva and Necrotic Skin Lesions of Pigs, with the Human Oral Pathogen Treponema denticola"

    Article Title: Genome-Wide Relatedness of Treponema pedis, from Gingiva and Necrotic Skin Lesions of Pigs, with the Human Oral Pathogen Treponema denticola

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0071281

    Circular representation of the T. pedis T A4 genome and complete genome alignment with T. denticola . (A.) Circular representation of the T. pedis T A4 genome. The CDSs are shown in violet where the outer circle represents predictions on the plus strand and the second circle those on the minus strand. CDSs with a best BLASTP hit in T. denticola ATCC 35405 are colored red and shown in the third circle. The fourth circle represents genes with best BLASTP hits in T. brennaborense (black), F. nucleatum (green), F. alocis (blue) and T. succinifaciens (grey). G+C skew is drawn in the inner circle. (B.) Complete genome alignment between T. pedis T A4 and T. denticola ATCC 35405. Dots represent maximum unique matches (MUMs) between the genomes. MUMs oriented in the same direction are depicted as red dots and reverse complemented MUMs are depicted as blue dots.
    Figure Legend Snippet: Circular representation of the T. pedis T A4 genome and complete genome alignment with T. denticola . (A.) Circular representation of the T. pedis T A4 genome. The CDSs are shown in violet where the outer circle represents predictions on the plus strand and the second circle those on the minus strand. CDSs with a best BLASTP hit in T. denticola ATCC 35405 are colored red and shown in the third circle. The fourth circle represents genes with best BLASTP hits in T. brennaborense (black), F. nucleatum (green), F. alocis (blue) and T. succinifaciens (grey). G+C skew is drawn in the inner circle. (B.) Complete genome alignment between T. pedis T A4 and T. denticola ATCC 35405. Dots represent maximum unique matches (MUMs) between the genomes. MUMs oriented in the same direction are depicted as red dots and reverse complemented MUMs are depicted as blue dots.

    Techniques Used:

    18) Product Images from "Disruption of a Type II Endonuclease (TDE0911) Enables Treponema denticola ATCC 35405 To Accept an Unmethylated Shuttle Vector ▿"

    Article Title: Disruption of a Type II Endonuclease (TDE0911) Enables Treponema denticola ATCC 35405 To Accept an Unmethylated Shuttle Vector ▿

    Journal: Applied and Environmental Microbiology

    doi: 10.1128/AEM.00417-11

    Transformation of pBFC into different T. denticola strains. Ten micrograms of methylated (mpBFC, top panels) or unmethylated pBFC plasmid (umpBFC, bottom panels) was electroporated into ATCC 35405, ATCC 33520, and the TdΔ911 mutant. Images were
    Figure Legend Snippet: Transformation of pBFC into different T. denticola strains. Ten micrograms of methylated (mpBFC, top panels) or unmethylated pBFC plasmid (umpBFC, bottom panels) was electroporated into ATCC 35405, ATCC 33520, and the TdΔ911 mutant. Images were

    Techniques Used: Transformation Assay, Methylation, Plasmid Preparation, Mutagenesis

    19) Product Images from "Composition and Localization of Treponema denticola Outer Membrane Complexes ▿"

    Article Title: Composition and Localization of Treponema denticola Outer Membrane Complexes ▿

    Journal: Infection and Immunity

    doi: 10.1128/IAI.05701-11

    Localization of T. denticola major surface protein and protease complex polypeptides. A surface localization immunofluorescence assay was performed with T. denticola ATCC 35405 with or without membrane permeabilization, using polyclonal antibodies raised
    Figure Legend Snippet: Localization of T. denticola major surface protein and protease complex polypeptides. A surface localization immunofluorescence assay was performed with T. denticola ATCC 35405 with or without membrane permeabilization, using polyclonal antibodies raised

    Techniques Used: Immunofluorescence

    20) Product Images from "Treponema denticola chymotrypsin-like proteinase (CTLP) integrates spirochaetes within oral microbial communities"

    Article Title: Treponema denticola chymotrypsin-like proteinase (CTLP) integrates spirochaetes within oral microbial communities

    Journal: Microbiology

    doi: 10.1099/mic.0.055939-0

    Role of the CTLP complex in the formation of T. denticola / P. gingivalis dual-species biofilms. Representative CLSM images of dual-species biofilms of (a, b) T. denticola ATCC 35405 and (c, d) T. denticola CKE, with P. gingivalis ATCC 33277. Biofilms were
    Figure Legend Snippet: Role of the CTLP complex in the formation of T. denticola / P. gingivalis dual-species biofilms. Representative CLSM images of dual-species biofilms of (a, b) T. denticola ATCC 35405 and (c, d) T. denticola CKE, with P. gingivalis ATCC 33277. Biofilms were

    Techniques Used: Confocal Laser Scanning Microscopy

    Adherence levels of Treponema to other periodontopathogens. The input cell number was 1.2×10 7 cells per well of T. denticola ATCC 35405 (black bars), T. denticola MHE (mid-grey bars), T. denticola CKE (dark-grey bars) and T. vincentii ATCC 35580
    Figure Legend Snippet: Adherence levels of Treponema to other periodontopathogens. The input cell number was 1.2×10 7 cells per well of T. denticola ATCC 35405 (black bars), T. denticola MHE (mid-grey bars), T. denticola CKE (dark-grey bars) and T. vincentii ATCC 35580

    Techniques Used:

    Fluorescence microscopy of monospecies or dual-species biofilms of T. denticola ATCC 35405, T. denticola CKE or T. denticola MHE, and P. gingivalis ATCC 33277, and corresponding biomass data. (a) Biofilms formed upon saliva-coated coverslips after 72
    Figure Legend Snippet: Fluorescence microscopy of monospecies or dual-species biofilms of T. denticola ATCC 35405, T. denticola CKE or T. denticola MHE, and P. gingivalis ATCC 33277, and corresponding biomass data. (a) Biofilms formed upon saliva-coated coverslips after 72

    Techniques Used: Fluorescence, Microscopy

    21) Product Images from "Filamentous Actin Disruption and Diminished Inositol Phosphate Response in Gingival Fibroblasts Caused by Treponema denticola"

    Article Title: Filamentous Actin Disruption and Diminished Inositol Phosphate Response in Gingival Fibroblasts Caused by Treponema denticola

    Journal: Infection and Immunity

    doi:

    Histogram of fluorescence intensity of rhodamine-phalloidin-labeled F-actin in HGF during a 140-min time course, analyzed by confocal microscopy. There was significant depolymerization of F-actin in the T. denticola ATCC 35405-challenged HGF (left graph) in comparison with the control HGF (right graph). The degree of diminished fluorescence in T. denticola -challenged cells was significant at 60 min ( P
    Figure Legend Snippet: Histogram of fluorescence intensity of rhodamine-phalloidin-labeled F-actin in HGF during a 140-min time course, analyzed by confocal microscopy. There was significant depolymerization of F-actin in the T. denticola ATCC 35405-challenged HGF (left graph) in comparison with the control HGF (right graph). The degree of diminished fluorescence in T. denticola -challenged cells was significant at 60 min ( P

    Techniques Used: Fluorescence, Labeling, Confocal Microscopy

    Comparison of filamentous actin disruption (mean ± standard deviation) in HGF challenged with different concentrations of whole cells of T. denticola ATCC 35405 (□) and OM extract (▪). The dry weight for the OM and the dry weight for the T. denticola cells were equivalent at each optical density (OD) point shown on the x axis.
    Figure Legend Snippet: Comparison of filamentous actin disruption (mean ± standard deviation) in HGF challenged with different concentrations of whole cells of T. denticola ATCC 35405 (□) and OM extract (▪). The dry weight for the OM and the dry weight for the T. denticola cells were equivalent at each optical density (OD) point shown on the x axis.

    Techniques Used: Standard Deviation

    Qualitative comparison by SDS-PAGE of T. denticola ATCC 35405 whole cells (lane 1), OM extract run at the same time (lane 2), and repeat of the OM extract run in a different gel to resolve mid-range bands more clearly (lane 3). The positions of molecular size standards (broad-range SDS-PAGE standards; Bio-Rad) are shown in kilodaltons at the left. Conditions were as follows: Washed T. denticola suspensions (optical density of 1.2 at 550 nm) from 3-day cultures or undiluted OM extract were mixed 1:1 with sample buffer (0.25 M Tris-HCl [pH 6.8], 20% glycerol, 4.6% SDS, 0.02% bromophenol blue, 10% β-mercaptoethanol) and boiled for 10 min; 25 μl was added to each lane of a 1-mm-thick Ready Gel (Bio-Rad) with a 4% stacking gel and 12% resolving gel. Electrophoresis was run in a Mini-Protean II cell (Bio-Rad). Whole cells and OM extract had several bands in common.
    Figure Legend Snippet: Qualitative comparison by SDS-PAGE of T. denticola ATCC 35405 whole cells (lane 1), OM extract run at the same time (lane 2), and repeat of the OM extract run in a different gel to resolve mid-range bands more clearly (lane 3). The positions of molecular size standards (broad-range SDS-PAGE standards; Bio-Rad) are shown in kilodaltons at the left. Conditions were as follows: Washed T. denticola suspensions (optical density of 1.2 at 550 nm) from 3-day cultures or undiluted OM extract were mixed 1:1 with sample buffer (0.25 M Tris-HCl [pH 6.8], 20% glycerol, 4.6% SDS, 0.02% bromophenol blue, 10% β-mercaptoethanol) and boiled for 10 min; 25 μl was added to each lane of a 1-mm-thick Ready Gel (Bio-Rad) with a 4% stacking gel and 12% resolving gel. Electrophoresis was run in a Mini-Protean II cell (Bio-Rad). Whole cells and OM extract had several bands in common.

    Techniques Used: SDS Page, Nucleic Acid Electrophoresis

    22) Product Images from "Filamentous Actin Disruption and Diminished Inositol Phosphate Response in Gingival Fibroblasts Caused by Treponema denticola"

    Article Title: Filamentous Actin Disruption and Diminished Inositol Phosphate Response in Gingival Fibroblasts Caused by Treponema denticola

    Journal: Infection and Immunity

    doi:

    Histogram of fluorescence intensity of rhodamine-phalloidin-labeled F-actin in HGF during a 140-min time course, analyzed by confocal microscopy. There was significant depolymerization of F-actin in the T. denticola ATCC 35405-challenged HGF (left graph) in comparison with the control HGF (right graph). The degree of diminished fluorescence in T. denticola -challenged cells was significant at 60 min ( P
    Figure Legend Snippet: Histogram of fluorescence intensity of rhodamine-phalloidin-labeled F-actin in HGF during a 140-min time course, analyzed by confocal microscopy. There was significant depolymerization of F-actin in the T. denticola ATCC 35405-challenged HGF (left graph) in comparison with the control HGF (right graph). The degree of diminished fluorescence in T. denticola -challenged cells was significant at 60 min ( P

    Techniques Used: Fluorescence, Labeling, Confocal Microscopy

    Comparison of filamentous actin disruption (mean ± standard deviation) in HGF challenged with different concentrations of whole cells of T. denticola ATCC 35405 (□) and OM extract (▪). The dry weight for the OM and the dry weight for the T. denticola cells were equivalent at each optical density (OD) point shown on the x axis.
    Figure Legend Snippet: Comparison of filamentous actin disruption (mean ± standard deviation) in HGF challenged with different concentrations of whole cells of T. denticola ATCC 35405 (□) and OM extract (▪). The dry weight for the OM and the dry weight for the T. denticola cells were equivalent at each optical density (OD) point shown on the x axis.

    Techniques Used: Standard Deviation

    Qualitative comparison by SDS-PAGE of T. denticola ATCC 35405 whole cells (lane 1), OM extract run at the same time (lane 2), and repeat of the OM extract run in a different gel to resolve mid-range bands more clearly (lane 3). The positions of molecular size standards (broad-range SDS-PAGE standards; Bio-Rad) are shown in kilodaltons at the left. Conditions were as follows: Washed T. denticola suspensions (optical density of 1.2 at 550 nm) from 3-day cultures or undiluted OM extract were mixed 1:1 with sample buffer (0.25 M Tris-HCl [pH 6.8], 20% glycerol, 4.6% SDS, 0.02% bromophenol blue, 10% β-mercaptoethanol) and boiled for 10 min; 25 μl was added to each lane of a 1-mm-thick Ready Gel (Bio-Rad) with a 4% stacking gel and 12% resolving gel. Electrophoresis was run in a Mini-Protean II cell (Bio-Rad). Whole cells and OM extract had several bands in common.
    Figure Legend Snippet: Qualitative comparison by SDS-PAGE of T. denticola ATCC 35405 whole cells (lane 1), OM extract run at the same time (lane 2), and repeat of the OM extract run in a different gel to resolve mid-range bands more clearly (lane 3). The positions of molecular size standards (broad-range SDS-PAGE standards; Bio-Rad) are shown in kilodaltons at the left. Conditions were as follows: Washed T. denticola suspensions (optical density of 1.2 at 550 nm) from 3-day cultures or undiluted OM extract were mixed 1:1 with sample buffer (0.25 M Tris-HCl [pH 6.8], 20% glycerol, 4.6% SDS, 0.02% bromophenol blue, 10% β-mercaptoethanol) and boiled for 10 min; 25 μl was added to each lane of a 1-mm-thick Ready Gel (Bio-Rad) with a 4% stacking gel and 12% resolving gel. Electrophoresis was run in a Mini-Protean II cell (Bio-Rad). Whole cells and OM extract had several bands in common.

    Techniques Used: SDS Page, Nucleic Acid Electrophoresis

    23) Product Images from "Filamentous Actin Disruption and Diminished Inositol Phosphate Response in Gingival Fibroblasts Caused by Treponema denticola"

    Article Title: Filamentous Actin Disruption and Diminished Inositol Phosphate Response in Gingival Fibroblasts Caused by Treponema denticola

    Journal: Infection and Immunity

    doi:

    Histogram of fluorescence intensity of rhodamine-phalloidin-labeled F-actin in HGF during a 140-min time course, analyzed by confocal microscopy. There was significant depolymerization of F-actin in the T. denticola ATCC 35405-challenged HGF (left graph) in comparison with the control HGF (right graph). The degree of diminished fluorescence in T. denticola -challenged cells was significant at 60 min ( P
    Figure Legend Snippet: Histogram of fluorescence intensity of rhodamine-phalloidin-labeled F-actin in HGF during a 140-min time course, analyzed by confocal microscopy. There was significant depolymerization of F-actin in the T. denticola ATCC 35405-challenged HGF (left graph) in comparison with the control HGF (right graph). The degree of diminished fluorescence in T. denticola -challenged cells was significant at 60 min ( P

    Techniques Used: Fluorescence, Labeling, Confocal Microscopy

    Comparison of filamentous actin disruption (mean ± standard deviation) in HGF challenged with different concentrations of whole cells of T. denticola ATCC 35405 (□) and OM extract (▪). The dry weight for the OM and the dry weight for the T. denticola cells were equivalent at each optical density (OD) point shown on the x axis.
    Figure Legend Snippet: Comparison of filamentous actin disruption (mean ± standard deviation) in HGF challenged with different concentrations of whole cells of T. denticola ATCC 35405 (□) and OM extract (▪). The dry weight for the OM and the dry weight for the T. denticola cells were equivalent at each optical density (OD) point shown on the x axis.

    Techniques Used: Standard Deviation

    Qualitative comparison by SDS-PAGE of T. denticola ATCC 35405 whole cells (lane 1), OM extract run at the same time (lane 2), and repeat of the OM extract run in a different gel to resolve mid-range bands more clearly (lane 3). The positions of molecular size standards (broad-range SDS-PAGE standards; Bio-Rad) are shown in kilodaltons at the left. Conditions were as follows: Washed T. denticola suspensions (optical density of 1.2 at 550 nm) from 3-day cultures or undiluted OM extract were mixed 1:1 with sample buffer (0.25 M Tris-HCl [pH 6.8], 20% glycerol, 4.6% SDS, 0.02% bromophenol blue, 10% β-mercaptoethanol) and boiled for 10 min; 25 μl was added to each lane of a 1-mm-thick Ready Gel (Bio-Rad) with a 4% stacking gel and 12% resolving gel. Electrophoresis was run in a Mini-Protean II cell (Bio-Rad). Whole cells and OM extract had several bands in common.
    Figure Legend Snippet: Qualitative comparison by SDS-PAGE of T. denticola ATCC 35405 whole cells (lane 1), OM extract run at the same time (lane 2), and repeat of the OM extract run in a different gel to resolve mid-range bands more clearly (lane 3). The positions of molecular size standards (broad-range SDS-PAGE standards; Bio-Rad) are shown in kilodaltons at the left. Conditions were as follows: Washed T. denticola suspensions (optical density of 1.2 at 550 nm) from 3-day cultures or undiluted OM extract were mixed 1:1 with sample buffer (0.25 M Tris-HCl [pH 6.8], 20% glycerol, 4.6% SDS, 0.02% bromophenol blue, 10% β-mercaptoethanol) and boiled for 10 min; 25 μl was added to each lane of a 1-mm-thick Ready Gel (Bio-Rad) with a 4% stacking gel and 12% resolving gel. Electrophoresis was run in a Mini-Protean II cell (Bio-Rad). Whole cells and OM extract had several bands in common.

    Techniques Used: SDS Page, Nucleic Acid Electrophoresis

    24) Product Images from "Filamentous Actin Disruption and Diminished Inositol Phosphate Response in Gingival Fibroblasts Caused by Treponema denticola"

    Article Title: Filamentous Actin Disruption and Diminished Inositol Phosphate Response in Gingival Fibroblasts Caused by Treponema denticola

    Journal: Infection and Immunity

    doi:

    Histogram of fluorescence intensity of rhodamine-phalloidin-labeled F-actin in HGF during a 140-min time course, analyzed by confocal microscopy. There was significant depolymerization of F-actin in the T. denticola ATCC 35405-challenged HGF (left graph) in comparison with the control HGF (right graph). The degree of diminished fluorescence in T. denticola -challenged cells was significant at 60 min ( P
    Figure Legend Snippet: Histogram of fluorescence intensity of rhodamine-phalloidin-labeled F-actin in HGF during a 140-min time course, analyzed by confocal microscopy. There was significant depolymerization of F-actin in the T. denticola ATCC 35405-challenged HGF (left graph) in comparison with the control HGF (right graph). The degree of diminished fluorescence in T. denticola -challenged cells was significant at 60 min ( P

    Techniques Used: Fluorescence, Labeling, Confocal Microscopy

    Comparison of filamentous actin disruption (mean ± standard deviation) in HGF challenged with different concentrations of whole cells of T. denticola ATCC 35405 (□) and OM extract (▪). The dry weight for the OM and the dry weight for the T. denticola cells were equivalent at each optical density (OD) point shown on the x axis.
    Figure Legend Snippet: Comparison of filamentous actin disruption (mean ± standard deviation) in HGF challenged with different concentrations of whole cells of T. denticola ATCC 35405 (□) and OM extract (▪). The dry weight for the OM and the dry weight for the T. denticola cells were equivalent at each optical density (OD) point shown on the x axis.

    Techniques Used: Standard Deviation

    Qualitative comparison by SDS-PAGE of T. denticola ATCC 35405 whole cells (lane 1), OM extract run at the same time (lane 2), and repeat of the OM extract run in a different gel to resolve mid-range bands more clearly (lane 3). The positions of molecular size standards (broad-range SDS-PAGE standards; Bio-Rad) are shown in kilodaltons at the left. Conditions were as follows: Washed T. denticola suspensions (optical density of 1.2 at 550 nm) from 3-day cultures or undiluted OM extract were mixed 1:1 with sample buffer (0.25 M Tris-HCl [pH 6.8], 20% glycerol, 4.6% SDS, 0.02% bromophenol blue, 10% β-mercaptoethanol) and boiled for 10 min; 25 μl was added to each lane of a 1-mm-thick Ready Gel (Bio-Rad) with a 4% stacking gel and 12% resolving gel. Electrophoresis was run in a Mini-Protean II cell (Bio-Rad). Whole cells and OM extract had several bands in common.
    Figure Legend Snippet: Qualitative comparison by SDS-PAGE of T. denticola ATCC 35405 whole cells (lane 1), OM extract run at the same time (lane 2), and repeat of the OM extract run in a different gel to resolve mid-range bands more clearly (lane 3). The positions of molecular size standards (broad-range SDS-PAGE standards; Bio-Rad) are shown in kilodaltons at the left. Conditions were as follows: Washed T. denticola suspensions (optical density of 1.2 at 550 nm) from 3-day cultures or undiluted OM extract were mixed 1:1 with sample buffer (0.25 M Tris-HCl [pH 6.8], 20% glycerol, 4.6% SDS, 0.02% bromophenol blue, 10% β-mercaptoethanol) and boiled for 10 min; 25 μl was added to each lane of a 1-mm-thick Ready Gel (Bio-Rad) with a 4% stacking gel and 12% resolving gel. Electrophoresis was run in a Mini-Protean II cell (Bio-Rad). Whole cells and OM extract had several bands in common.

    Techniques Used: SDS Page, Nucleic Acid Electrophoresis

    25) Product Images from "Filamentous Actin Disruption and Diminished Inositol Phosphate Response in Gingival Fibroblasts Caused by Treponema denticola"

    Article Title: Filamentous Actin Disruption and Diminished Inositol Phosphate Response in Gingival Fibroblasts Caused by Treponema denticola

    Journal: Infection and Immunity

    doi:

    Histogram of fluorescence intensity of rhodamine-phalloidin-labeled F-actin in HGF during a 140-min time course, analyzed by confocal microscopy. There was significant depolymerization of F-actin in the T. denticola ATCC 35405-challenged HGF (left graph) in comparison with the control HGF (right graph). The degree of diminished fluorescence in T. denticola -challenged cells was significant at 60 min ( P
    Figure Legend Snippet: Histogram of fluorescence intensity of rhodamine-phalloidin-labeled F-actin in HGF during a 140-min time course, analyzed by confocal microscopy. There was significant depolymerization of F-actin in the T. denticola ATCC 35405-challenged HGF (left graph) in comparison with the control HGF (right graph). The degree of diminished fluorescence in T. denticola -challenged cells was significant at 60 min ( P

    Techniques Used: Fluorescence, Labeling, Confocal Microscopy

    Comparison of filamentous actin disruption (mean ± standard deviation) in HGF challenged with different concentrations of whole cells of T. denticola ATCC 35405 (□) and OM extract (▪). The dry weight for the OM and the dry weight for the T. denticola cells were equivalent at each optical density (OD) point shown on the x axis.
    Figure Legend Snippet: Comparison of filamentous actin disruption (mean ± standard deviation) in HGF challenged with different concentrations of whole cells of T. denticola ATCC 35405 (□) and OM extract (▪). The dry weight for the OM and the dry weight for the T. denticola cells were equivalent at each optical density (OD) point shown on the x axis.

    Techniques Used: Standard Deviation

    Qualitative comparison by SDS-PAGE of T. denticola ATCC 35405 whole cells (lane 1), OM extract run at the same time (lane 2), and repeat of the OM extract run in a different gel to resolve mid-range bands more clearly (lane 3). The positions of molecular size standards (broad-range SDS-PAGE standards; Bio-Rad) are shown in kilodaltons at the left. Conditions were as follows: Washed T. denticola suspensions (optical density of 1.2 at 550 nm) from 3-day cultures or undiluted OM extract were mixed 1:1 with sample buffer (0.25 M Tris-HCl [pH 6.8], 20% glycerol, 4.6% SDS, 0.02% bromophenol blue, 10% β-mercaptoethanol) and boiled for 10 min; 25 μl was added to each lane of a 1-mm-thick Ready Gel (Bio-Rad) with a 4% stacking gel and 12% resolving gel. Electrophoresis was run in a Mini-Protean II cell (Bio-Rad). Whole cells and OM extract had several bands in common.
    Figure Legend Snippet: Qualitative comparison by SDS-PAGE of T. denticola ATCC 35405 whole cells (lane 1), OM extract run at the same time (lane 2), and repeat of the OM extract run in a different gel to resolve mid-range bands more clearly (lane 3). The positions of molecular size standards (broad-range SDS-PAGE standards; Bio-Rad) are shown in kilodaltons at the left. Conditions were as follows: Washed T. denticola suspensions (optical density of 1.2 at 550 nm) from 3-day cultures or undiluted OM extract were mixed 1:1 with sample buffer (0.25 M Tris-HCl [pH 6.8], 20% glycerol, 4.6% SDS, 0.02% bromophenol blue, 10% β-mercaptoethanol) and boiled for 10 min; 25 μl was added to each lane of a 1-mm-thick Ready Gel (Bio-Rad) with a 4% stacking gel and 12% resolving gel. Electrophoresis was run in a Mini-Protean II cell (Bio-Rad). Whole cells and OM extract had several bands in common.

    Techniques Used: SDS Page, Nucleic Acid Electrophoresis

    26) Product Images from "Characterization of a potential ABC-type bacteriocin exporter protein from Treponema denticola"

    Article Title: Characterization of a potential ABC-type bacteriocin exporter protein from Treponema denticola

    Journal: BMC Oral Health

    doi: 10.1186/s12903-016-0243-7

    Southern blot analysis of tepA1 ( a ), tepA2 ( b ) , and tepA3 ( c ). Genomic DNA from T. denticola strains was digested with Hin dIII. 1: genomic DNA from ATCC 33520, 2: genomic DNA from ATCC 33521, genomic DNA from ATCC 35404, 4: genomic DNA from ATCC 35405, 5: genomic DNA from GM1
    Figure Legend Snippet: Southern blot analysis of tepA1 ( a ), tepA2 ( b ) , and tepA3 ( c ). Genomic DNA from T. denticola strains was digested with Hin dIII. 1: genomic DNA from ATCC 33520, 2: genomic DNA from ATCC 33521, genomic DNA from ATCC 35404, 4: genomic DNA from ATCC 35405, 5: genomic DNA from GM1

    Techniques Used: Southern Blot

    27) Product Images from "Characterization of a potential ABC-type bacteriocin exporter protein from Treponema denticola"

    Article Title: Characterization of a potential ABC-type bacteriocin exporter protein from Treponema denticola

    Journal: BMC Oral Health

    doi: 10.1186/s12903-016-0243-7

    Southern blot analysis of tepA1 ( a ), tepA2 ( b ) , and tepA3 ( c ). Genomic DNA from T. denticola strains was digested with Hin dIII. 1: genomic DNA from ATCC 33520, 2: genomic DNA from ATCC 33521, genomic DNA from ATCC 35404, 4: genomic DNA from ATCC 35405, 5: genomic DNA from GM1
    Figure Legend Snippet: Southern blot analysis of tepA1 ( a ), tepA2 ( b ) , and tepA3 ( c ). Genomic DNA from T. denticola strains was digested with Hin dIII. 1: genomic DNA from ATCC 33520, 2: genomic DNA from ATCC 33521, genomic DNA from ATCC 35404, 4: genomic DNA from ATCC 35405, 5: genomic DNA from GM1

    Techniques Used: Southern Blot

    28) Product Images from "The Chymotrypsin-Like Protease Complex of Treponema denticola ATCC 35405 Mediates Fibrinogen Adherence and Degradation ▿"

    Article Title: The Chymotrypsin-Like Protease Complex of Treponema denticola ATCC 35405 Mediates Fibrinogen Adherence and Degradation ▿

    Journal: Infection and Immunity

    doi: 10.1128/IAI.00258-07

    TCT in the absence or presence of T. denticola ATCC 35405, MHE (Msp − ), or CKE (CTLP − ). Human plasma was incubated with T. denticola (1.2 × 10 9 cells/ml) suspended in PBS or with PBS alone (control) for 5 min before the addition
    Figure Legend Snippet: TCT in the absence or presence of T. denticola ATCC 35405, MHE (Msp − ), or CKE (CTLP − ). Human plasma was incubated with T. denticola (1.2 × 10 9 cells/ml) suspended in PBS or with PBS alone (control) for 5 min before the addition

    Techniques Used: Incubation

    Fibrinogen zymograms of outer membrane proteins from T. denticola ATCC 35405, MHE (Msp − ), and CKE (CTLP − ). Triton X-114 extracts were incubated for 5 min at 20°C (−) or 100°C (+) before being subjected to
    Figure Legend Snippet: Fibrinogen zymograms of outer membrane proteins from T. denticola ATCC 35405, MHE (Msp − ), and CKE (CTLP − ). Triton X-114 extracts were incubated for 5 min at 20°C (−) or 100°C (+) before being subjected to

    Techniques Used: Incubation

    Purification and enzymatic activity of major fibrinogen-binding protein from T. denticola ATCC 35405. Outer membrane proteins were extracted with 0.1% Triton X-114 solution and incubated with fibrinogen-linked Sepharose, and then tightly bound
    Figure Legend Snippet: Purification and enzymatic activity of major fibrinogen-binding protein from T. denticola ATCC 35405. Outer membrane proteins were extracted with 0.1% Triton X-114 solution and incubated with fibrinogen-linked Sepharose, and then tightly bound

    Techniques Used: Purification, Activity Assay, Binding Assay, Incubation

    Binding of fluid-phase or immobilized fibrinogen by T. denticola ATCC 35405 (⧫), MHE (Msp − ; ▴), or CKE (CTLP − ; ▪). (A and B) Treponema cells immobilized onto plastic wells in the absence (A) or presence (B) of 0.05
    Figure Legend Snippet: Binding of fluid-phase or immobilized fibrinogen by T. denticola ATCC 35405 (⧫), MHE (Msp − ; ▴), or CKE (CTLP − ; ▪). (A and B) Treponema cells immobilized onto plastic wells in the absence (A) or presence (B) of 0.05

    Techniques Used: Binding Assay

    Fibrinogen blot overlay of outer membrane protein extracts from T. denticola ATCC 35405, MHE, and CKE. Proteins were extracted with 1% Triton X-114 and incubated for 5 min at 20°C (−) or 100°C (+) before being subjected
    Figure Legend Snippet: Fibrinogen blot overlay of outer membrane protein extracts from T. denticola ATCC 35405, MHE, and CKE. Proteins were extracted with 1% Triton X-114 and incubated for 5 min at 20°C (−) or 100°C (+) before being subjected

    Techniques Used: Incubation

    Adherence of T. denticola ATCC 35405 cells to denatured fibrinogen or recombinant fibrinogen polypeptides. (A) Human fibrinogen (N) or purified recombinant Aα, Bβ, and γ chain polypeptides were heated for 5 min at 100°C
    Figure Legend Snippet: Adherence of T. denticola ATCC 35405 cells to denatured fibrinogen or recombinant fibrinogen polypeptides. (A) Human fibrinogen (N) or purified recombinant Aα, Bβ, and γ chain polypeptides were heated for 5 min at 100°C

    Techniques Used: Recombinant, Purification

    29) Product Images from "The Chymotrypsin-Like Protease Complex of Treponema denticola ATCC 35405 Mediates Fibrinogen Adherence and Degradation ▿"

    Article Title: The Chymotrypsin-Like Protease Complex of Treponema denticola ATCC 35405 Mediates Fibrinogen Adherence and Degradation ▿

    Journal: Infection and Immunity

    doi: 10.1128/IAI.00258-07

    TCT in the absence or presence of T. denticola ATCC 35405, MHE (Msp − ), or CKE (CTLP − ). Human plasma was incubated with T. denticola (1.2 × 10 9 cells/ml) suspended in PBS or with PBS alone (control) for 5 min before the addition
    Figure Legend Snippet: TCT in the absence or presence of T. denticola ATCC 35405, MHE (Msp − ), or CKE (CTLP − ). Human plasma was incubated with T. denticola (1.2 × 10 9 cells/ml) suspended in PBS or with PBS alone (control) for 5 min before the addition

    Techniques Used: Incubation

    Fibrinogen zymograms of outer membrane proteins from T. denticola ATCC 35405, MHE (Msp − ), and CKE (CTLP − ). Triton X-114 extracts were incubated for 5 min at 20°C (−) or 100°C (+) before being subjected to
    Figure Legend Snippet: Fibrinogen zymograms of outer membrane proteins from T. denticola ATCC 35405, MHE (Msp − ), and CKE (CTLP − ). Triton X-114 extracts were incubated for 5 min at 20°C (−) or 100°C (+) before being subjected to

    Techniques Used: Incubation

    Purification and enzymatic activity of major fibrinogen-binding protein from T. denticola ATCC 35405. Outer membrane proteins were extracted with 0.1% Triton X-114 solution and incubated with fibrinogen-linked Sepharose, and then tightly bound
    Figure Legend Snippet: Purification and enzymatic activity of major fibrinogen-binding protein from T. denticola ATCC 35405. Outer membrane proteins were extracted with 0.1% Triton X-114 solution and incubated with fibrinogen-linked Sepharose, and then tightly bound

    Techniques Used: Purification, Activity Assay, Binding Assay, Incubation

    Binding of fluid-phase or immobilized fibrinogen by T. denticola ATCC 35405 (⧫), MHE (Msp − ; ▴), or CKE (CTLP − ; ▪). (A and B) Treponema cells immobilized onto plastic wells in the absence (A) or presence (B) of 0.05
    Figure Legend Snippet: Binding of fluid-phase or immobilized fibrinogen by T. denticola ATCC 35405 (⧫), MHE (Msp − ; ▴), or CKE (CTLP − ; ▪). (A and B) Treponema cells immobilized onto plastic wells in the absence (A) or presence (B) of 0.05

    Techniques Used: Binding Assay

    Fibrinogen blot overlay of outer membrane protein extracts from T. denticola ATCC 35405, MHE, and CKE. Proteins were extracted with 1% Triton X-114 and incubated for 5 min at 20°C (−) or 100°C (+) before being subjected
    Figure Legend Snippet: Fibrinogen blot overlay of outer membrane protein extracts from T. denticola ATCC 35405, MHE, and CKE. Proteins were extracted with 1% Triton X-114 and incubated for 5 min at 20°C (−) or 100°C (+) before being subjected

    Techniques Used: Incubation

    Adherence of T. denticola ATCC 35405 cells to denatured fibrinogen or recombinant fibrinogen polypeptides. (A) Human fibrinogen (N) or purified recombinant Aα, Bβ, and γ chain polypeptides were heated for 5 min at 100°C
    Figure Legend Snippet: Adherence of T. denticola ATCC 35405 cells to denatured fibrinogen or recombinant fibrinogen polypeptides. (A) Human fibrinogen (N) or purified recombinant Aα, Bβ, and γ chain polypeptides were heated for 5 min at 100°C

    Techniques Used: Recombinant, Purification

    30) Product Images from "The Chymotrypsin-Like Protease Complex of Treponema denticola ATCC 35405 Mediates Fibrinogen Adherence and Degradation ▿"

    Article Title: The Chymotrypsin-Like Protease Complex of Treponema denticola ATCC 35405 Mediates Fibrinogen Adherence and Degradation ▿

    Journal: Infection and Immunity

    doi: 10.1128/IAI.00258-07

    TCT in the absence or presence of T. denticola ATCC 35405, MHE (Msp − ), or CKE (CTLP − ). Human plasma was incubated with T. denticola (1.2 × 10 9 cells/ml) suspended in PBS or with PBS alone (control) for 5 min before the addition
    Figure Legend Snippet: TCT in the absence or presence of T. denticola ATCC 35405, MHE (Msp − ), or CKE (CTLP − ). Human plasma was incubated with T. denticola (1.2 × 10 9 cells/ml) suspended in PBS or with PBS alone (control) for 5 min before the addition

    Techniques Used: Incubation

    Fibrinogen zymograms of outer membrane proteins from T. denticola ATCC 35405, MHE (Msp − ), and CKE (CTLP − ). Triton X-114 extracts were incubated for 5 min at 20°C (−) or 100°C (+) before being subjected to
    Figure Legend Snippet: Fibrinogen zymograms of outer membrane proteins from T. denticola ATCC 35405, MHE (Msp − ), and CKE (CTLP − ). Triton X-114 extracts were incubated for 5 min at 20°C (−) or 100°C (+) before being subjected to

    Techniques Used: Incubation

    Purification and enzymatic activity of major fibrinogen-binding protein from T. denticola ATCC 35405. Outer membrane proteins were extracted with 0.1% Triton X-114 solution and incubated with fibrinogen-linked Sepharose, and then tightly bound
    Figure Legend Snippet: Purification and enzymatic activity of major fibrinogen-binding protein from T. denticola ATCC 35405. Outer membrane proteins were extracted with 0.1% Triton X-114 solution and incubated with fibrinogen-linked Sepharose, and then tightly bound

    Techniques Used: Purification, Activity Assay, Binding Assay, Incubation

    Binding of fluid-phase or immobilized fibrinogen by T. denticola ATCC 35405 (⧫), MHE (Msp − ; ▴), or CKE (CTLP − ; ▪). (A and B) Treponema cells immobilized onto plastic wells in the absence (A) or presence (B) of 0.05
    Figure Legend Snippet: Binding of fluid-phase or immobilized fibrinogen by T. denticola ATCC 35405 (⧫), MHE (Msp − ; ▴), or CKE (CTLP − ; ▪). (A and B) Treponema cells immobilized onto plastic wells in the absence (A) or presence (B) of 0.05

    Techniques Used: Binding Assay

    Fibrinogen blot overlay of outer membrane protein extracts from T. denticola ATCC 35405, MHE, and CKE. Proteins were extracted with 1% Triton X-114 and incubated for 5 min at 20°C (−) or 100°C (+) before being subjected
    Figure Legend Snippet: Fibrinogen blot overlay of outer membrane protein extracts from T. denticola ATCC 35405, MHE, and CKE. Proteins were extracted with 1% Triton X-114 and incubated for 5 min at 20°C (−) or 100°C (+) before being subjected

    Techniques Used: Incubation

    Adherence of T. denticola ATCC 35405 cells to denatured fibrinogen or recombinant fibrinogen polypeptides. (A) Human fibrinogen (N) or purified recombinant Aα, Bβ, and γ chain polypeptides were heated for 5 min at 100°C
    Figure Legend Snippet: Adherence of T. denticola ATCC 35405 cells to denatured fibrinogen or recombinant fibrinogen polypeptides. (A) Human fibrinogen (N) or purified recombinant Aα, Bβ, and γ chain polypeptides were heated for 5 min at 100°C

    Techniques Used: Recombinant, Purification

    31) Product Images from "Binding Properties and Adhesion-Mediating Regions of the Major Sheath Protein of Treponema denticola ATCC 35405"

    Article Title: Binding Properties and Adhesion-Mediating Regions of the Major Sheath Protein of Treponema denticola ATCC 35405

    Journal: Infection and Immunity

    doi: 10.1128/IAI.73.5.2891-2898.2005

    Interactions of rMsp antibodies with T. denticola ATCC 35405 cells and of whole-cell antibodies with rMsp fragments. (Panel A) Reactivity in ELISA of antiserum (1:250 diluted) to T. denticola ATCC 35405 cells (W) or antisera (1:250 diluted) raised to
    Figure Legend Snippet: Interactions of rMsp antibodies with T. denticola ATCC 35405 cells and of whole-cell antibodies with rMsp fragments. (Panel A) Reactivity in ELISA of antiserum (1:250 diluted) to T. denticola ATCC 35405 cells (W) or antisera (1:250 diluted) raised to

    Techniques Used: Enzyme-linked Immunosorbent Assay

    Reactivities of Msp antisera with T. denticola ATCC 35405 outer membrane protein extracts. (Panel A) SDS-PAGE gel of outer membrane proteins. (Panel B) Western blots reacted with antisera to rN-Msp (lane 1), rV-Msp (lane 2), or rC-Msp (lane 3). Molecular
    Figure Legend Snippet: Reactivities of Msp antisera with T. denticola ATCC 35405 outer membrane protein extracts. (Panel A) SDS-PAGE gel of outer membrane proteins. (Panel B) Western blots reacted with antisera to rN-Msp (lane 1), rV-Msp (lane 2), or rC-Msp (lane 3). Molecular

    Techniques Used: SDS Page, Western Blot

    Binding of rMsp to human fibronectin and to 30-kDa N-terminal fragment of human fibronectin. (Panel A) Western blot overlay of trypsin-derived fragments of human plasma fibronectin reacted with rMsp (lane 1) or with biotinylated T. denticola ATCC 35405
    Figure Legend Snippet: Binding of rMsp to human fibronectin and to 30-kDa N-terminal fragment of human fibronectin. (Panel A) Western blot overlay of trypsin-derived fragments of human plasma fibronectin reacted with rMsp (lane 1) or with biotinylated T. denticola ATCC 35405

    Techniques Used: Binding Assay, Western Blot, Derivative Assay

    Diagrammatic representation of the Msp sequences from T. denticola ATCC 35520 (A), strain ATCC 35405 (B), and of recombinant Msp polypeptides rMsp (530 aa residues), rN-Msp (189 aa residues), rV-Msp (57 aa residues), and rN-Msp (272 aa residues), with
    Figure Legend Snippet: Diagrammatic representation of the Msp sequences from T. denticola ATCC 35520 (A), strain ATCC 35405 (B), and of recombinant Msp polypeptides rMsp (530 aa residues), rN-Msp (189 aa residues), rV-Msp (57 aa residues), and rN-Msp (272 aa residues), with

    Techniques Used: Recombinant

    Effect of exogenously added rMsp on adhesion of Treponema strains to immobilized human fibronectin or 30-kDa fibronectin fragment. (Panel A) Adhesion levels of T. denticola ATCC 35405 cells to 0.1 μg fibronectin (filled column) or 30-kDa fibronectin
    Figure Legend Snippet: Effect of exogenously added rMsp on adhesion of Treponema strains to immobilized human fibronectin or 30-kDa fibronectin fragment. (Panel A) Adhesion levels of T. denticola ATCC 35405 cells to 0.1 μg fibronectin (filled column) or 30-kDa fibronectin

    Techniques Used:

    32) Product Images from "In vitro-activity of oily calcium hydroxide suspension on microorganisms as well as on human alveolar osteoblasts and periodontal ligament fibroblasts"

    Article Title: In vitro-activity of oily calcium hydroxide suspension on microorganisms as well as on human alveolar osteoblasts and periodontal ligament fibroblasts

    Journal: BMC Oral Health

    doi: 10.1186/1472-6831-14-9

    Attachment of A) HAO cells and B) PDL fibroblasts (mean and SD) 4 h after coverage with and without oily calcium hydroxide suspension (OCHS) and addition of A. actinomycetemcomitans Y4 as well as the combination of P. gingivalis ATCC 33277, T. forsythia ATCC 43037, T. denticola ATCC 35405 (p-values in comparison with controls and with no OCHS respectively each were determined by Student’s t-test).
    Figure Legend Snippet: Attachment of A) HAO cells and B) PDL fibroblasts (mean and SD) 4 h after coverage with and without oily calcium hydroxide suspension (OCHS) and addition of A. actinomycetemcomitans Y4 as well as the combination of P. gingivalis ATCC 33277, T. forsythia ATCC 43037, T. denticola ATCC 35405 (p-values in comparison with controls and with no OCHS respectively each were determined by Student’s t-test).

    Techniques Used:

    33) Product Images from "Disruption of a Type II Endonuclease (TDE0911) Enables Treponema denticola ATCC 35405 To Accept an Unmethylated Shuttle Vector ▿"

    Article Title: Disruption of a Type II Endonuclease (TDE0911) Enables Treponema denticola ATCC 35405 To Accept an Unmethylated Shuttle Vector ▿

    Journal: Applied and Environmental Microbiology

    doi: 10.1128/AEM.00417-11

    Transformation of pBFC into different T. denticola strains. Ten micrograms of methylated (mpBFC, top panels) or unmethylated pBFC plasmid (umpBFC, bottom panels) was electroporated into ATCC 35405, ATCC 33520, and the TdΔ911 mutant. Images were
    Figure Legend Snippet: Transformation of pBFC into different T. denticola strains. Ten micrograms of methylated (mpBFC, top panels) or unmethylated pBFC plasmid (umpBFC, bottom panels) was electroporated into ATCC 35405, ATCC 33520, and the TdΔ911 mutant. Images were

    Techniques Used: Transformation Assay, Methylation, Plasmid Preparation, Mutagenesis

    34) Product Images from "Treponema denticola chymotrypsin-like proteinase (CTLP) integrates spirochaetes within oral microbial communities"

    Article Title: Treponema denticola chymotrypsin-like proteinase (CTLP) integrates spirochaetes within oral microbial communities

    Journal: Microbiology

    doi: 10.1099/mic.0.055939-0

    Role of the CTLP complex in the formation of T. denticola / P. gingivalis dual-species biofilms. Representative CLSM images of dual-species biofilms of (a, b) T. denticola ATCC 35405 and (c, d) T. denticola CKE, with P. gingivalis ATCC 33277. Biofilms were
    Figure Legend Snippet: Role of the CTLP complex in the formation of T. denticola / P. gingivalis dual-species biofilms. Representative CLSM images of dual-species biofilms of (a, b) T. denticola ATCC 35405 and (c, d) T. denticola CKE, with P. gingivalis ATCC 33277. Biofilms were

    Techniques Used: Confocal Laser Scanning Microscopy

    Adherence levels of Treponema to other periodontopathogens. The input cell number was 1.2×10 7 cells per well of T. denticola ATCC 35405 (black bars), T. denticola MHE (mid-grey bars), T. denticola CKE (dark-grey bars) and T. vincentii ATCC 35580
    Figure Legend Snippet: Adherence levels of Treponema to other periodontopathogens. The input cell number was 1.2×10 7 cells per well of T. denticola ATCC 35405 (black bars), T. denticola MHE (mid-grey bars), T. denticola CKE (dark-grey bars) and T. vincentii ATCC 35580

    Techniques Used:

    Fluorescence microscopy of monospecies or dual-species biofilms of T. denticola ATCC 35405, T. denticola CKE or T. denticola MHE, and P. gingivalis ATCC 33277, and corresponding biomass data. (a) Biofilms formed upon saliva-coated coverslips after 72
    Figure Legend Snippet: Fluorescence microscopy of monospecies or dual-species biofilms of T. denticola ATCC 35405, T. denticola CKE or T. denticola MHE, and P. gingivalis ATCC 33277, and corresponding biomass data. (a) Biofilms formed upon saliva-coated coverslips after 72

    Techniques Used: Fluorescence, Microscopy

    35) Product Images from "Dentipain, a Streptococcus-pyogenes-IdeS-protease homologue, is a novel virulence factor of Treponema denticola"

    Article Title: Dentipain, a Streptococcus-pyogenes-IdeS-protease homologue, is a novel virulence factor of Treponema denticola

    Journal: Biological chemistry

    doi: 10.1515/BC.2010.113

    Construction of an IdeT protease-deficient mutant A . (i) The wild-type ideT locus detailing the four protein domains; (ii) pIDEKO4, constructed using pMCL191, two ideT PCR generated fragments flanking the proteolytic domain (hatched bar and dotted bar) and an erythromycin resistance cassette derived from pVA2198. The restriction sites introduced during PCR are also shown; (iii) the ideT mutant locus detailing the dentipain region replaced with an erythromycin resistance cassette by homologous recombination. B . (i) PCR amplification of the ideT locus using primers ID-1 and ID-4, which amplify from amino acid residues 172 to 640. Lane 1, T. denticola ATCC 35405; lane 2, T. denticola IDEKO4; lane 3, T. denticola Ide5; lane 4, T. denticola Ide6; lane 5 , Molecular size marker. (ii) PCR amplification of the ideT locus using primers ID-1 and CATU, which amplify from amino acid residues 172 to 417. Lane 1, T. denticola ATCC 35405; lane 2, T. denticola IDEKO4; lane 3 , Molecular size marker.
    Figure Legend Snippet: Construction of an IdeT protease-deficient mutant A . (i) The wild-type ideT locus detailing the four protein domains; (ii) pIDEKO4, constructed using pMCL191, two ideT PCR generated fragments flanking the proteolytic domain (hatched bar and dotted bar) and an erythromycin resistance cassette derived from pVA2198. The restriction sites introduced during PCR are also shown; (iii) the ideT mutant locus detailing the dentipain region replaced with an erythromycin resistance cassette by homologous recombination. B . (i) PCR amplification of the ideT locus using primers ID-1 and ID-4, which amplify from amino acid residues 172 to 640. Lane 1, T. denticola ATCC 35405; lane 2, T. denticola IDEKO4; lane 3, T. denticola Ide5; lane 4, T. denticola Ide6; lane 5 , Molecular size marker. (ii) PCR amplification of the ideT locus using primers ID-1 and CATU, which amplify from amino acid residues 172 to 417. Lane 1, T. denticola ATCC 35405; lane 2, T. denticola IDEKO4; lane 3 , Molecular size marker.

    Techniques Used: Mutagenesis, Construct, Polymerase Chain Reaction, Generated, Derivative Assay, Homologous Recombination, Amplification, Marker

    Analysis of IdeT translation A. SDS-PAGE of T. denticola sonicates. Lane 1, T. denticola ATCC 35405 sonicate; lane 2, T. denticola IDEKO4 sonicate. B. Immunoblot analysis of IdeT from T. denticola cells. Lane 1, T. denticola ATCC 35405 sonicate; lane 2, T. denticola IDEKO4 sonicate. Antibody: rabbit serum anti-IdeT recombinant protein (219–647). The arrow indicates the band which reacted with this antibody. C. SDS-PAGE of concentrated culture supernatant of T. denticola . Culture supernatant of T. denticola grown in E-TYGV medium was collected and concentrated. Lane 1, culture supernatant of T. denticola ATCC 35405; lane 2, culture supernatant of T. denticola IDEKO4. D. Immunoblot analysis of IdeT in culture supernatants. Lane 1, culture supernatant of T. denticola ATCC 35405; lane 2, culture supernatant of T. denticola IDEKO4. Antibody: rabbit serum anti-IdeT recombinant protein (219–647). The arrow indicates the band which reacted with this antibody. E. Immunoblot analysis of IdeT in culture supernatants. Lane 1, culture supernatant of T. denticola ATCC 3540 5; lane 2, culture supernatant of T. denticola IDEK O4. Antibody : rabbit serum anti-IdeT synthetic peptide (IdeT498–511). The arrow indicates the band which reacted with this antibody.
    Figure Legend Snippet: Analysis of IdeT translation A. SDS-PAGE of T. denticola sonicates. Lane 1, T. denticola ATCC 35405 sonicate; lane 2, T. denticola IDEKO4 sonicate. B. Immunoblot analysis of IdeT from T. denticola cells. Lane 1, T. denticola ATCC 35405 sonicate; lane 2, T. denticola IDEKO4 sonicate. Antibody: rabbit serum anti-IdeT recombinant protein (219–647). The arrow indicates the band which reacted with this antibody. C. SDS-PAGE of concentrated culture supernatant of T. denticola . Culture supernatant of T. denticola grown in E-TYGV medium was collected and concentrated. Lane 1, culture supernatant of T. denticola ATCC 35405; lane 2, culture supernatant of T. denticola IDEKO4. D. Immunoblot analysis of IdeT in culture supernatants. Lane 1, culture supernatant of T. denticola ATCC 35405; lane 2, culture supernatant of T. denticola IDEKO4. Antibody: rabbit serum anti-IdeT recombinant protein (219–647). The arrow indicates the band which reacted with this antibody. E. Immunoblot analysis of IdeT in culture supernatants. Lane 1, culture supernatant of T. denticola ATCC 3540 5; lane 2, culture supernatant of T. denticola IDEK O4. Antibody : rabbit serum anti-IdeT synthetic peptide (IdeT498–511). The arrow indicates the band which reacted with this antibody.

    Techniques Used: SDS Page, Recombinant

    Analysis of the role of IdeT proteolytic activity in the virulence of T. denticola . Bars represent the mean area of lesions at the infection sites following challenge with either T. denticola ATCC 35405 or T. denticola IDEKO4. Mice were injected with live T. denticola ATCC 35405 (black bars) or IDEKO4 (open bars), and lesion areas determined at the indicated times following infection. Bars indicate standard deviation. *P
    Figure Legend Snippet: Analysis of the role of IdeT proteolytic activity in the virulence of T. denticola . Bars represent the mean area of lesions at the infection sites following challenge with either T. denticola ATCC 35405 or T. denticola IDEKO4. Mice were injected with live T. denticola ATCC 35405 (black bars) or IDEKO4 (open bars), and lesion areas determined at the indicated times following infection. Bars indicate standard deviation. *P

    Techniques Used: Activity Assay, Infection, Mouse Assay, Injection, Standard Deviation

    36) Product Images from "The opdB Locus Encodes the Trypsin-Like Peptidase Activity of Treponema denticola"

    Article Title: The opdB Locus Encodes the Trypsin-Like Peptidase Activity of Treponema denticola

    Journal: Infection and Immunity

    doi: 10.1128/IAI.69.10.6193-6200.2001

    SDS-PAGE analysis of T. denticola ATCC 35405 and opdB mutant BAE whole-cell extracts. Molecular mass standards are shown in the left lane. Arrow, band at approximately 78 kDa that is present in ATCC 35405 and that appears to be missing in BAE. This is consistent with the predicted molecular mass of the OpdB peptide.
    Figure Legend Snippet: SDS-PAGE analysis of T. denticola ATCC 35405 and opdB mutant BAE whole-cell extracts. Molecular mass standards are shown in the left lane. Arrow, band at approximately 78 kDa that is present in ATCC 35405 and that appears to be missing in BAE. This is consistent with the predicted molecular mass of the OpdB peptide.

    Techniques Used: SDS Page, Mutagenesis

    Confirmation of opdB mutant construction. (A) PCR amplification of opdB in T. denticola ATCC 35405 and isogenic opdB mutant BAE. Genomic DNAs were subjected to PCR using primers CX203 and CX204. (B) Southern blot analysis of T. denticola ATCC 35405 and isogenic opdB mutant BAE. Genomic DNAs were digested with Hin dIII and hybridized with a biotinylated internal fragment of opdB or the Sac I- Acc I fragment of ermF/AM . The ermF/AM cassette contains a single Hin dIII site.
    Figure Legend Snippet: Confirmation of opdB mutant construction. (A) PCR amplification of opdB in T. denticola ATCC 35405 and isogenic opdB mutant BAE. Genomic DNAs were subjected to PCR using primers CX203 and CX204. (B) Southern blot analysis of T. denticola ATCC 35405 and isogenic opdB mutant BAE. Genomic DNAs were digested with Hin dIII and hybridized with a biotinylated internal fragment of opdB or the Sac I- Acc I fragment of ermF/AM . The ermF/AM cassette contains a single Hin dIII site.

    Techniques Used: Mutagenesis, Polymerase Chain Reaction, Amplification, Southern Blot

    Growth of T. denticola ATCC 35405 and isogenic opdB mutant BAE. Bacteria were inoculated in NOS media and incubated under anaerobic conditions. A 600 was measured every 8 h for 5 days and every 24 h for the next 5 days. Error bars represent the range of A 600 values obtained from triplicate samples.
    Figure Legend Snippet: Growth of T. denticola ATCC 35405 and isogenic opdB mutant BAE. Bacteria were inoculated in NOS media and incubated under anaerobic conditions. A 600 was measured every 8 h for 5 days and every 24 h for the next 5 days. Error bars represent the range of A 600 values obtained from triplicate samples.

    Techniques Used: Mutagenesis, Incubation

    Enzymatic activities of T. denticola ATCC 35405 and opdB mutant BAE. (A) Trypsin-like activity measured by BA p NA hydrolysis. (B) Chymotrypsin-like activity measured by SAA p NA hydrolysis. NOS media, culture medium negative control. Vertical bars show standard deviations of triplicate samples. (C) API-ZYM strip. Tested enzymes: 1, control; 2, alkaline phosphatase; 3, esterase; 4, esterase lipase; 5, lipase; 6, leucine arylamidase; 7, valine arylamidase; 8, cystine arylamidase; 9, trypsin; 10, α-chymotrypsin; 11, acid phosphatase; 12, naphthol-AS-BI-phosphohydrolase; 13, α-galactosidase; 14, β-galactosidase; 15, β-glucuronidase; 16, α-glucosidase; 17, β-glucosidase; 18, N -acetyl-β-glucosaminidase; 19, α-mannosidase; 20, α-fucosidase. Arrow, substrate for the trypsin assay (BANA).
    Figure Legend Snippet: Enzymatic activities of T. denticola ATCC 35405 and opdB mutant BAE. (A) Trypsin-like activity measured by BA p NA hydrolysis. (B) Chymotrypsin-like activity measured by SAA p NA hydrolysis. NOS media, culture medium negative control. Vertical bars show standard deviations of triplicate samples. (C) API-ZYM strip. Tested enzymes: 1, control; 2, alkaline phosphatase; 3, esterase; 4, esterase lipase; 5, lipase; 6, leucine arylamidase; 7, valine arylamidase; 8, cystine arylamidase; 9, trypsin; 10, α-chymotrypsin; 11, acid phosphatase; 12, naphthol-AS-BI-phosphohydrolase; 13, α-galactosidase; 14, β-galactosidase; 15, β-glucuronidase; 16, α-glucosidase; 17, β-glucosidase; 18, N -acetyl-β-glucosaminidase; 19, α-mannosidase; 20, α-fucosidase. Arrow, substrate for the trypsin assay (BANA).

    Techniques Used: Mutagenesis, Activity Assay, Negative Control, Stripping Membranes

    37) Product Images from "Dentilisin Activity Affects the Organization of the Outer Sheath of Treponema denticola"

    Article Title: Dentilisin Activity Affects the Organization of the Outer Sheath of Treponema denticola

    Journal: Journal of Bacteriology

    doi:

    Mean areas of lesions at infection sites after challenge with T. denticola ATCC 35405 and prtP mutant K1. Mice were injected with live T. denticola ATCC 35405 (open bars) or mutant K1 (hatched bars), and lesion areas were determined at the indicated times following infection.
    Figure Legend Snippet: Mean areas of lesions at infection sites after challenge with T. denticola ATCC 35405 and prtP mutant K1. Mice were injected with live T. denticola ATCC 35405 (open bars) or mutant K1 (hatched bars), and lesion areas were determined at the indicated times following infection.

    Techniques Used: Infection, Mutagenesis, Mouse Assay, Injection

    Immunoblot analysis of T. denticola ATCC 35405 and K1 with anti- T. denticola ATCC 35405 whole-cell serum. Samples from lanes 1 to 4 were treated with PMSF. Lanes 1 and 5, T. denticola ATCC 35405 (without boiling); lanes 2 and 6, T. denticola K1 (without boiling); lanes 3 and 7, T. denticola ATCC 35405 (with boiling); lanes 4 and 8, T. denticola K1 (with boiling). Arrowheads indicate the high-molecular-mass oligomeric protein and the Msp band.
    Figure Legend Snippet: Immunoblot analysis of T. denticola ATCC 35405 and K1 with anti- T. denticola ATCC 35405 whole-cell serum. Samples from lanes 1 to 4 were treated with PMSF. Lanes 1 and 5, T. denticola ATCC 35405 (without boiling); lanes 2 and 6, T. denticola K1 (without boiling); lanes 3 and 7, T. denticola ATCC 35405 (with boiling); lanes 4 and 8, T. denticola K1 (with boiling). Arrowheads indicate the high-molecular-mass oligomeric protein and the Msp band.

    Techniques Used:

    Southern blot analysis of T. denticola ATCC 35405 and prtP mutant K1. Chromosomal DNAs from T. denticola ATCC 35405 (lanes 1 and 3) and prtP mutant K1 (lanes 2 and 4) were digested with Hin dIII and hybridized with a digoxigenin-labeled Kpn I- Pst I fragment from the prtP gene (lanes 1 and 2) or the Kpn I- Bam HI fragment from pVA2198 (lanes 3 and 4). Numbers at right are kilobase pairs.
    Figure Legend Snippet: Southern blot analysis of T. denticola ATCC 35405 and prtP mutant K1. Chromosomal DNAs from T. denticola ATCC 35405 (lanes 1 and 3) and prtP mutant K1 (lanes 2 and 4) were digested with Hin dIII and hybridized with a digoxigenin-labeled Kpn I- Pst I fragment from the prtP gene (lanes 1 and 2) or the Kpn I- Bam HI fragment from pVA2198 (lanes 3 and 4). Numbers at right are kilobase pairs.

    Techniques Used: Southern Blot, Mutagenesis, Labeling

    Gelatin zymography of sonicates of T. denticola ATCC 35405 (lane 1) and K1 (lane 2).
    Figure Legend Snippet: Gelatin zymography of sonicates of T. denticola ATCC 35405 (lane 1) and K1 (lane 2).

    Techniques Used: Zymography

    SDS-PAGE analysis of sonicates of T. denticola ATCC 35405 and K1. Samples from lanes 1 to 4 were treated with PMSF. Lanes 1 and 5, T. denticola ATCC 35405 (without boiling); lanes 2 and 6, T. denticola K1 (without boiling); lanes 3 and 7, T. denticola ATCC 35405 (with boiling); lanes 4 and 8, T. denticola K1 (with boiling). After electrophoresis, the gel was stained with Coomassie brilliant blue R-250. Arrowheads indicate the high-molecular-mass oligomeric protein and the Msp band.
    Figure Legend Snippet: SDS-PAGE analysis of sonicates of T. denticola ATCC 35405 and K1. Samples from lanes 1 to 4 were treated with PMSF. Lanes 1 and 5, T. denticola ATCC 35405 (without boiling); lanes 2 and 6, T. denticola K1 (without boiling); lanes 3 and 7, T. denticola ATCC 35405 (with boiling); lanes 4 and 8, T. denticola K1 (with boiling). After electrophoresis, the gel was stained with Coomassie brilliant blue R-250. Arrowheads indicate the high-molecular-mass oligomeric protein and the Msp band.

    Techniques Used: SDS Page, Electrophoresis, Staining

    Immunoblot analysis of T. denticola ATCC 35405 (lane 1; boiled) and K1 (lane 2; boiled) with antidentilisin serum.
    Figure Legend Snippet: Immunoblot analysis of T. denticola ATCC 35405 (lane 1; boiled) and K1 (lane 2; boiled) with antidentilisin serum.

    Techniques Used:

    38) Product Images from "Filamentous Actin Disruption and Diminished Inositol Phosphate Response in Gingival Fibroblasts Caused by Treponema denticola"

    Article Title: Filamentous Actin Disruption and Diminished Inositol Phosphate Response in Gingival Fibroblasts Caused by Treponema denticola

    Journal: Infection and Immunity

    doi:

    Histogram of fluorescence intensity of rhodamine-phalloidin-labeled F-actin in HGF during a 140-min time course, analyzed by confocal microscopy. There was significant depolymerization of F-actin in the T. denticola ATCC 35405-challenged HGF (left graph) in comparison with the control HGF (right graph). The degree of diminished fluorescence in T. denticola -challenged cells was significant at 60 min ( P
    Figure Legend Snippet: Histogram of fluorescence intensity of rhodamine-phalloidin-labeled F-actin in HGF during a 140-min time course, analyzed by confocal microscopy. There was significant depolymerization of F-actin in the T. denticola ATCC 35405-challenged HGF (left graph) in comparison with the control HGF (right graph). The degree of diminished fluorescence in T. denticola -challenged cells was significant at 60 min ( P

    Techniques Used: Fluorescence, Labeling, Confocal Microscopy

    Comparison of filamentous actin disruption (mean ± standard deviation) in HGF challenged with different concentrations of whole cells of T. denticola ATCC 35405 (□) and OM extract (▪). The dry weight for the OM and the dry weight for the T. denticola cells were equivalent at each optical density (OD) point shown on the x axis.
    Figure Legend Snippet: Comparison of filamentous actin disruption (mean ± standard deviation) in HGF challenged with different concentrations of whole cells of T. denticola ATCC 35405 (□) and OM extract (▪). The dry weight for the OM and the dry weight for the T. denticola cells were equivalent at each optical density (OD) point shown on the x axis.

    Techniques Used: Standard Deviation

    Qualitative comparison by SDS-PAGE of T. denticola ATCC 35405 whole cells (lane 1), OM extract run at the same time (lane 2), and repeat of the OM extract run in a different gel to resolve mid-range bands more clearly (lane 3). The positions of molecular size standards (broad-range SDS-PAGE standards; Bio-Rad) are shown in kilodaltons at the left. Conditions were as follows: Washed T. denticola suspensions (optical density of 1.2 at 550 nm) from 3-day cultures or undiluted OM extract were mixed 1:1 with sample buffer (0.25 M Tris-HCl [pH 6.8], 20% glycerol, 4.6% SDS, 0.02% bromophenol blue, 10% β-mercaptoethanol) and boiled for 10 min; 25 μl was added to each lane of a 1-mm-thick Ready Gel (Bio-Rad) with a 4% stacking gel and 12% resolving gel. Electrophoresis was run in a Mini-Protean II cell (Bio-Rad). Whole cells and OM extract had several bands in common.
    Figure Legend Snippet: Qualitative comparison by SDS-PAGE of T. denticola ATCC 35405 whole cells (lane 1), OM extract run at the same time (lane 2), and repeat of the OM extract run in a different gel to resolve mid-range bands more clearly (lane 3). The positions of molecular size standards (broad-range SDS-PAGE standards; Bio-Rad) are shown in kilodaltons at the left. Conditions were as follows: Washed T. denticola suspensions (optical density of 1.2 at 550 nm) from 3-day cultures or undiluted OM extract were mixed 1:1 with sample buffer (0.25 M Tris-HCl [pH 6.8], 20% glycerol, 4.6% SDS, 0.02% bromophenol blue, 10% β-mercaptoethanol) and boiled for 10 min; 25 μl was added to each lane of a 1-mm-thick Ready Gel (Bio-Rad) with a 4% stacking gel and 12% resolving gel. Electrophoresis was run in a Mini-Protean II cell (Bio-Rad). Whole cells and OM extract had several bands in common.

    Techniques Used: SDS Page, Nucleic Acid Electrophoresis

    39) Product Images from "Filamentous Actin Disruption and Diminished Inositol Phosphate Response in Gingival Fibroblasts Caused by Treponema denticola"

    Article Title: Filamentous Actin Disruption and Diminished Inositol Phosphate Response in Gingival Fibroblasts Caused by Treponema denticola

    Journal: Infection and Immunity

    doi:

    Histogram of fluorescence intensity of rhodamine-phalloidin-labeled F-actin in HGF during a 140-min time course, analyzed by confocal microscopy. There was significant depolymerization of F-actin in the T. denticola ATCC 35405-challenged HGF (left graph) in comparison with the control HGF (right graph). The degree of diminished fluorescence in T. denticola -challenged cells was significant at 60 min ( P
    Figure Legend Snippet: Histogram of fluorescence intensity of rhodamine-phalloidin-labeled F-actin in HGF during a 140-min time course, analyzed by confocal microscopy. There was significant depolymerization of F-actin in the T. denticola ATCC 35405-challenged HGF (left graph) in comparison with the control HGF (right graph). The degree of diminished fluorescence in T. denticola -challenged cells was significant at 60 min ( P

    Techniques Used: Fluorescence, Labeling, Confocal Microscopy

    Comparison of filamentous actin disruption (mean ± standard deviation) in HGF challenged with different concentrations of whole cells of T. denticola ATCC 35405 (□) and OM extract (▪). The dry weight for the OM and the dry weight for the T. denticola cells were equivalent at each optical density (OD) point shown on the x axis.
    Figure Legend Snippet: Comparison of filamentous actin disruption (mean ± standard deviation) in HGF challenged with different concentrations of whole cells of T. denticola ATCC 35405 (□) and OM extract (▪). The dry weight for the OM and the dry weight for the T. denticola cells were equivalent at each optical density (OD) point shown on the x axis.

    Techniques Used: Standard Deviation

    Qualitative comparison by SDS-PAGE of T. denticola ATCC 35405 whole cells (lane 1), OM extract run at the same time (lane 2), and repeat of the OM extract run in a different gel to resolve mid-range bands more clearly (lane 3). The positions of molecular size standards (broad-range SDS-PAGE standards; Bio-Rad) are shown in kilodaltons at the left. Conditions were as follows: Washed T. denticola suspensions (optical density of 1.2 at 550 nm) from 3-day cultures or undiluted OM extract were mixed 1:1 with sample buffer (0.25 M Tris-HCl [pH 6.8], 20% glycerol, 4.6% SDS, 0.02% bromophenol blue, 10% β-mercaptoethanol) and boiled for 10 min; 25 μl was added to each lane of a 1-mm-thick Ready Gel (Bio-Rad) with a 4% stacking gel and 12% resolving gel. Electrophoresis was run in a Mini-Protean II cell (Bio-Rad). Whole cells and OM extract had several bands in common.
    Figure Legend Snippet: Qualitative comparison by SDS-PAGE of T. denticola ATCC 35405 whole cells (lane 1), OM extract run at the same time (lane 2), and repeat of the OM extract run in a different gel to resolve mid-range bands more clearly (lane 3). The positions of molecular size standards (broad-range SDS-PAGE standards; Bio-Rad) are shown in kilodaltons at the left. Conditions were as follows: Washed T. denticola suspensions (optical density of 1.2 at 550 nm) from 3-day cultures or undiluted OM extract were mixed 1:1 with sample buffer (0.25 M Tris-HCl [pH 6.8], 20% glycerol, 4.6% SDS, 0.02% bromophenol blue, 10% β-mercaptoethanol) and boiled for 10 min; 25 μl was added to each lane of a 1-mm-thick Ready Gel (Bio-Rad) with a 4% stacking gel and 12% resolving gel. Electrophoresis was run in a Mini-Protean II cell (Bio-Rad). Whole cells and OM extract had several bands in common.

    Techniques Used: SDS Page, Nucleic Acid Electrophoresis

    40) Product Images from "Immunotopological Analysis of the Treponema denticola Major Surface Protein (Msp)"

    Article Title: Immunotopological Analysis of the Treponema denticola Major Surface Protein (Msp)

    Journal: Journal of Bacteriology

    doi: 10.1128/JB.00528-18

    Immunofluorescence microscopy of T. denticola , revealing the Msp surface domain. T. denticola ATCC 35405 and ATCC 33520, grown to an OD 600 of 0.2, were fixed on glass slides with 1% paraformaldehyde, incubated with PBS or PBS plus 0.5% Triton X-100, and probed with rabbit antibodies to native ATCC 35405 Msp or recombinant FlaA, followed by goat anti-rabbit IgG conjugated to Alexa Fluor 568 (Msp) or Alexa Fluor 488 (FlaA), or with DAPI. Images were obtained at a magnification of 600× using an Olympus BX40 microscope fitted with an Olympus DP73 camera.
    Figure Legend Snippet: Immunofluorescence microscopy of T. denticola , revealing the Msp surface domain. T. denticola ATCC 35405 and ATCC 33520, grown to an OD 600 of 0.2, were fixed on glass slides with 1% paraformaldehyde, incubated with PBS or PBS plus 0.5% Triton X-100, and probed with rabbit antibodies to native ATCC 35405 Msp or recombinant FlaA, followed by goat anti-rabbit IgG conjugated to Alexa Fluor 568 (Msp) or Alexa Fluor 488 (FlaA), or with DAPI. Images were obtained at a magnification of 600× using an Olympus BX40 microscope fitted with an Olympus DP73 camera.

    Techniques Used: Immunofluorescence, Microscopy, Incubation, Recombinant

    Map and immunoblots of deletion mutations made in msp for expression in E. coli . (Upper) The 543-residue Msp protein, with the signal peptide (SP) cleavage site indicated (residue 20), is shown above the deletions made in the coding region. The amino acid residues deleted in the N-terminal region in each of the three constructs are indicated. Deletions in the central region within the approximate boundaries of the central domain (D1 through D2) include predicted antigenic domains (Ag1 and Ag2), the remaining region of greatest divergence between Msps of strains ATCC 35405 and ATCC 33520 (Xr), and D2. These mutant Msps were expressed in E. coli . (Lower) Immunoblots of E. coli strains expressing full-length Msps with the indicated Msp residues deleted are shown. T. denticola ATCC 35405 serves as a positive control. Blots were probed with rabbit polyclonal antibodies raised against native ATCC 35405 Msp, the Msp N-terminal domain, or whole T. denticola (Td) cells. All samples were boiled prior to electrophoresis. Lanes contain lysates of E. coli strains. Antibodies raised against native T. denticola ATCC 35405 Msp or whole T. denticola ATCC 35405 cells do not recognize recombinant Msps lacking residues 229 to 251.
    Figure Legend Snippet: Map and immunoblots of deletion mutations made in msp for expression in E. coli . (Upper) The 543-residue Msp protein, with the signal peptide (SP) cleavage site indicated (residue 20), is shown above the deletions made in the coding region. The amino acid residues deleted in the N-terminal region in each of the three constructs are indicated. Deletions in the central region within the approximate boundaries of the central domain (D1 through D2) include predicted antigenic domains (Ag1 and Ag2), the remaining region of greatest divergence between Msps of strains ATCC 35405 and ATCC 33520 (Xr), and D2. These mutant Msps were expressed in E. coli . (Lower) Immunoblots of E. coli strains expressing full-length Msps with the indicated Msp residues deleted are shown. T. denticola ATCC 35405 serves as a positive control. Blots were probed with rabbit polyclonal antibodies raised against native ATCC 35405 Msp, the Msp N-terminal domain, or whole T. denticola (Td) cells. All samples were boiled prior to electrophoresis. Lanes contain lysates of E. coli strains. Antibodies raised against native T. denticola ATCC 35405 Msp or whole T. denticola ATCC 35405 cells do not recognize recombinant Msps lacking residues 229 to 251.

    Techniques Used: Western Blot, Expressing, Construct, Mutagenesis, Positive Control, Electrophoresis, Recombinant

    Models for T. denticola ATCC 35405 Msp generated by I-TASSER. The I-TASSER algorithm generates 5 predicted structural models based on several parameters, of which model 1 is the overall best model. Overall model ranking does not necessarily follow the C scores for proteins lacking closely related known structures. All 5 models are displayed to show the N termini (blue) and C termini (red). The ATCC 35405 Msp surface-exposed epitope (residues 229 to 251) is highlighted in green in each model. (A) Models 1 to 5 generated using the PDB data available in June 2017. (B) Models 1 to 5 generated using the PDB data available in October 2018.
    Figure Legend Snippet: Models for T. denticola ATCC 35405 Msp generated by I-TASSER. The I-TASSER algorithm generates 5 predicted structural models based on several parameters, of which model 1 is the overall best model. Overall model ranking does not necessarily follow the C scores for proteins lacking closely related known structures. All 5 models are displayed to show the N termini (blue) and C termini (red). The ATCC 35405 Msp surface-exposed epitope (residues 229 to 251) is highlighted in green in each model. (A) Models 1 to 5 generated using the PDB data available in June 2017. (B) Models 1 to 5 generated using the PDB data available in October 2018.

    Techniques Used: Generated

    41) Product Images from "Characterization of a potential ABC-type bacteriocin exporter protein from Treponema denticola"

    Article Title: Characterization of a potential ABC-type bacteriocin exporter protein from Treponema denticola

    Journal: BMC Oral Health

    doi: 10.1186/s12903-016-0243-7

    Southern blot analysis of tepA1 ( a ), tepA2 ( b ) , and tepA3 ( c ). Genomic DNA from T. denticola strains was digested with Hin dIII. 1: genomic DNA from ATCC 33520, 2: genomic DNA from ATCC 33521, genomic DNA from ATCC 35404, 4: genomic DNA from ATCC 35405, 5: genomic DNA from GM1
    Figure Legend Snippet: Southern blot analysis of tepA1 ( a ), tepA2 ( b ) , and tepA3 ( c ). Genomic DNA from T. denticola strains was digested with Hin dIII. 1: genomic DNA from ATCC 33520, 2: genomic DNA from ATCC 33521, genomic DNA from ATCC 35404, 4: genomic DNA from ATCC 35405, 5: genomic DNA from GM1

    Techniques Used: Southern Blot

    42) Product Images from "The Chymotrypsin-Like Protease Complex of Treponema denticola ATCC 35405 Mediates Fibrinogen Adherence and Degradation ▿"

    Article Title: The Chymotrypsin-Like Protease Complex of Treponema denticola ATCC 35405 Mediates Fibrinogen Adherence and Degradation ▿

    Journal: Infection and Immunity

    doi: 10.1128/IAI.00258-07

    TCT in the absence or presence of T. denticola ATCC 35405, MHE (Msp − ), or CKE (CTLP − ). Human plasma was incubated with T. denticola (1.2 × 10 9 cells/ml) suspended in PBS or with PBS alone (control) for 5 min before the addition
    Figure Legend Snippet: TCT in the absence or presence of T. denticola ATCC 35405, MHE (Msp − ), or CKE (CTLP − ). Human plasma was incubated with T. denticola (1.2 × 10 9 cells/ml) suspended in PBS or with PBS alone (control) for 5 min before the addition

    Techniques Used: Incubation

    Fibrinogen zymograms of outer membrane proteins from T. denticola ATCC 35405, MHE (Msp − ), and CKE (CTLP − ). Triton X-114 extracts were incubated for 5 min at 20°C (−) or 100°C (+) before being subjected to
    Figure Legend Snippet: Fibrinogen zymograms of outer membrane proteins from T. denticola ATCC 35405, MHE (Msp − ), and CKE (CTLP − ). Triton X-114 extracts were incubated for 5 min at 20°C (−) or 100°C (+) before being subjected to

    Techniques Used: Incubation

    Purification and enzymatic activity of major fibrinogen-binding protein from T. denticola ATCC 35405. Outer membrane proteins were extracted with 0.1% Triton X-114 solution and incubated with fibrinogen-linked Sepharose, and then tightly bound
    Figure Legend Snippet: Purification and enzymatic activity of major fibrinogen-binding protein from T. denticola ATCC 35405. Outer membrane proteins were extracted with 0.1% Triton X-114 solution and incubated with fibrinogen-linked Sepharose, and then tightly bound

    Techniques Used: Purification, Activity Assay, Binding Assay, Incubation

    Binding of fluid-phase or immobilized fibrinogen by T. denticola ATCC 35405 (⧫), MHE (Msp − ; ▴), or CKE (CTLP − ; ▪). (A and B) Treponema cells immobilized onto plastic wells in the absence (A) or presence (B) of 0.05
    Figure Legend Snippet: Binding of fluid-phase or immobilized fibrinogen by T. denticola ATCC 35405 (⧫), MHE (Msp − ; ▴), or CKE (CTLP − ; ▪). (A and B) Treponema cells immobilized onto plastic wells in the absence (A) or presence (B) of 0.05

    Techniques Used: Binding Assay

    Fibrinogen blot overlay of outer membrane protein extracts from T. denticola ATCC 35405, MHE, and CKE. Proteins were extracted with 1% Triton X-114 and incubated for 5 min at 20°C (−) or 100°C (+) before being subjected
    Figure Legend Snippet: Fibrinogen blot overlay of outer membrane protein extracts from T. denticola ATCC 35405, MHE, and CKE. Proteins were extracted with 1% Triton X-114 and incubated for 5 min at 20°C (−) or 100°C (+) before being subjected

    Techniques Used: Incubation

    Adherence of T. denticola ATCC 35405 cells to denatured fibrinogen or recombinant fibrinogen polypeptides. (A) Human fibrinogen (N) or purified recombinant Aα, Bβ, and γ chain polypeptides were heated for 5 min at 100°C
    Figure Legend Snippet: Adherence of T. denticola ATCC 35405 cells to denatured fibrinogen or recombinant fibrinogen polypeptides. (A) Human fibrinogen (N) or purified recombinant Aα, Bβ, and γ chain polypeptides were heated for 5 min at 100°C

    Techniques Used: Recombinant, Purification

    43) Product Images from "Genome-Wide Relatedness of Treponema pedis, from Gingiva and Necrotic Skin Lesions of Pigs, with the Human Oral Pathogen Treponema denticola"

    Article Title: Genome-Wide Relatedness of Treponema pedis, from Gingiva and Necrotic Skin Lesions of Pigs, with the Human Oral Pathogen Treponema denticola

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0071281

    Circular representation of the T. pedis T A4 genome and complete genome alignment with T. denticola . (A.) Circular representation of the T. pedis T A4 genome. The CDSs are shown in violet where the outer circle represents predictions on the plus strand and the second circle those on the minus strand. CDSs with a best BLASTP hit in T. denticola ATCC 35405 are colored red and shown in the third circle. The fourth circle represents genes with best BLASTP hits in T. brennaborense (black), F. nucleatum (green), F. alocis (blue) and T. succinifaciens (grey). G+C skew is drawn in the inner circle. (B.) Complete genome alignment between T. pedis T A4 and T. denticola ATCC 35405. Dots represent maximum unique matches (MUMs) between the genomes. MUMs oriented in the same direction are depicted as red dots and reverse complemented MUMs are depicted as blue dots.
    Figure Legend Snippet: Circular representation of the T. pedis T A4 genome and complete genome alignment with T. denticola . (A.) Circular representation of the T. pedis T A4 genome. The CDSs are shown in violet where the outer circle represents predictions on the plus strand and the second circle those on the minus strand. CDSs with a best BLASTP hit in T. denticola ATCC 35405 are colored red and shown in the third circle. The fourth circle represents genes with best BLASTP hits in T. brennaborense (black), F. nucleatum (green), F. alocis (blue) and T. succinifaciens (grey). G+C skew is drawn in the inner circle. (B.) Complete genome alignment between T. pedis T A4 and T. denticola ATCC 35405. Dots represent maximum unique matches (MUMs) between the genomes. MUMs oriented in the same direction are depicted as red dots and reverse complemented MUMs are depicted as blue dots.

    Techniques Used:

    44) Product Images from "Genome-Wide Relatedness of Treponema pedis, from Gingiva and Necrotic Skin Lesions of Pigs, with the Human Oral Pathogen Treponema denticola"

    Article Title: Genome-Wide Relatedness of Treponema pedis, from Gingiva and Necrotic Skin Lesions of Pigs, with the Human Oral Pathogen Treponema denticola

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0071281

    Circular representation of the T. pedis T A4 genome and complete genome alignment with T. denticola . (A.) Circular representation of the T. pedis T A4 genome. The CDSs are shown in violet where the outer circle represents predictions on the plus strand and the second circle those on the minus strand. CDSs with a best BLASTP hit in T. denticola ATCC 35405 are colored red and shown in the third circle. The fourth circle represents genes with best BLASTP hits in T. brennaborense (black), F. nucleatum (green), F. alocis (blue) and T. succinifaciens (grey). G+C skew is drawn in the inner circle. (B.) Complete genome alignment between T. pedis T A4 and T. denticola ATCC 35405. Dots represent maximum unique matches (MUMs) between the genomes. MUMs oriented in the same direction are depicted as red dots and reverse complemented MUMs are depicted as blue dots.
    Figure Legend Snippet: Circular representation of the T. pedis T A4 genome and complete genome alignment with T. denticola . (A.) Circular representation of the T. pedis T A4 genome. The CDSs are shown in violet where the outer circle represents predictions on the plus strand and the second circle those on the minus strand. CDSs with a best BLASTP hit in T. denticola ATCC 35405 are colored red and shown in the third circle. The fourth circle represents genes with best BLASTP hits in T. brennaborense (black), F. nucleatum (green), F. alocis (blue) and T. succinifaciens (grey). G+C skew is drawn in the inner circle. (B.) Complete genome alignment between T. pedis T A4 and T. denticola ATCC 35405. Dots represent maximum unique matches (MUMs) between the genomes. MUMs oriented in the same direction are depicted as red dots and reverse complemented MUMs are depicted as blue dots.

    Techniques Used:

    45) Product Images from "Involvement of Toll-Like Receptors 2 and 4 in the Innate Immune Response to Treponema denticola and Its Outer Sheath Components "

    Article Title: Involvement of Toll-Like Receptors 2 and 4 in the Innate Immune Response to Treponema denticola and Its Outer Sheath Components

    Journal: Infection and Immunity

    doi: 10.1128/IAI.00488-09

    Protein identification by tandem mass spectrometry. Both samples matched the MSP of T. denticola ATCC 35405. Panels: A, 110- to 150-kDa band (Fig. ); B, MSP-enriched preparation. Calculated pI, 6.34. Nominal masses ( M r s), 58,703 and 58,233
    Figure Legend Snippet: Protein identification by tandem mass spectrometry. Both samples matched the MSP of T. denticola ATCC 35405. Panels: A, 110- to 150-kDa band (Fig. ); B, MSP-enriched preparation. Calculated pI, 6.34. Nominal masses ( M r s), 58,703 and 58,233

    Techniques Used: Mass Spectrometry

    46) Product Images from "Dentilisin Activity Affects the Organization of the Outer Sheath of Treponema denticola"

    Article Title: Dentilisin Activity Affects the Organization of the Outer Sheath of Treponema denticola

    Journal: Journal of Bacteriology

    doi:

    Mean areas of lesions at infection sites after challenge with T. denticola ATCC 35405 and prtP mutant K1. Mice were injected with live T. denticola ATCC 35405 (open bars) or mutant K1 (hatched bars), and lesion areas were determined at the indicated times following infection.
    Figure Legend Snippet: Mean areas of lesions at infection sites after challenge with T. denticola ATCC 35405 and prtP mutant K1. Mice were injected with live T. denticola ATCC 35405 (open bars) or mutant K1 (hatched bars), and lesion areas were determined at the indicated times following infection.

    Techniques Used: Infection, Mutagenesis, Mouse Assay, Injection

    Immunoblot analysis of T. denticola ATCC 35405 and K1 with anti- T. denticola ATCC 35405 whole-cell serum. Samples from lanes 1 to 4 were treated with PMSF. Lanes 1 and 5, T. denticola ATCC 35405 (without boiling); lanes 2 and 6, T. denticola K1 (without boiling); lanes 3 and 7, T. denticola ATCC 35405 (with boiling); lanes 4 and 8, T. denticola K1 (with boiling). Arrowheads indicate the high-molecular-mass oligomeric protein and the Msp band.
    Figure Legend Snippet: Immunoblot analysis of T. denticola ATCC 35405 and K1 with anti- T. denticola ATCC 35405 whole-cell serum. Samples from lanes 1 to 4 were treated with PMSF. Lanes 1 and 5, T. denticola ATCC 35405 (without boiling); lanes 2 and 6, T. denticola K1 (without boiling); lanes 3 and 7, T. denticola ATCC 35405 (with boiling); lanes 4 and 8, T. denticola K1 (with boiling). Arrowheads indicate the high-molecular-mass oligomeric protein and the Msp band.

    Techniques Used:

    Southern blot analysis of T. denticola ATCC 35405 and prtP mutant K1. Chromosomal DNAs from T. denticola ATCC 35405 (lanes 1 and 3) and prtP mutant K1 (lanes 2 and 4) were digested with Hin dIII and hybridized with a digoxigenin-labeled Kpn I- Pst I fragment from the prtP gene (lanes 1 and 2) or the Kpn I- Bam HI fragment from pVA2198 (lanes 3 and 4). Numbers at right are kilobase pairs.
    Figure Legend Snippet: Southern blot analysis of T. denticola ATCC 35405 and prtP mutant K1. Chromosomal DNAs from T. denticola ATCC 35405 (lanes 1 and 3) and prtP mutant K1 (lanes 2 and 4) were digested with Hin dIII and hybridized with a digoxigenin-labeled Kpn I- Pst I fragment from the prtP gene (lanes 1 and 2) or the Kpn I- Bam HI fragment from pVA2198 (lanes 3 and 4). Numbers at right are kilobase pairs.

    Techniques Used: Southern Blot, Mutagenesis, Labeling

    Gelatin zymography of sonicates of T. denticola ATCC 35405 (lane 1) and K1 (lane 2).
    Figure Legend Snippet: Gelatin zymography of sonicates of T. denticola ATCC 35405 (lane 1) and K1 (lane 2).

    Techniques Used: Zymography

    SDS-PAGE analysis of sonicates of T. denticola ATCC 35405 and K1. Samples from lanes 1 to 4 were treated with PMSF. Lanes 1 and 5, T. denticola ATCC 35405 (without boiling); lanes 2 and 6, T. denticola K1 (without boiling); lanes 3 and 7, T. denticola ATCC 35405 (with boiling); lanes 4 and 8, T. denticola K1 (with boiling). After electrophoresis, the gel was stained with Coomassie brilliant blue R-250. Arrowheads indicate the high-molecular-mass oligomeric protein and the Msp band.
    Figure Legend Snippet: SDS-PAGE analysis of sonicates of T. denticola ATCC 35405 and K1. Samples from lanes 1 to 4 were treated with PMSF. Lanes 1 and 5, T. denticola ATCC 35405 (without boiling); lanes 2 and 6, T. denticola K1 (without boiling); lanes 3 and 7, T. denticola ATCC 35405 (with boiling); lanes 4 and 8, T. denticola K1 (with boiling). After electrophoresis, the gel was stained with Coomassie brilliant blue R-250. Arrowheads indicate the high-molecular-mass oligomeric protein and the Msp band.

    Techniques Used: SDS Page, Electrophoresis, Staining

    Immunoblot analysis of T. denticola ATCC 35405 (lane 1; boiled) and K1 (lane 2; boiled) with antidentilisin serum.
    Figure Legend Snippet: Immunoblot analysis of T. denticola ATCC 35405 (lane 1; boiled) and K1 (lane 2; boiled) with antidentilisin serum.

    Techniques Used:

    47) Product Images from "Dentilisin Activity Affects the Organization of the Outer Sheath of Treponema denticola"

    Article Title: Dentilisin Activity Affects the Organization of the Outer Sheath of Treponema denticola

    Journal: Journal of Bacteriology

    doi:

    Mean areas of lesions at infection sites after challenge with T. denticola ATCC 35405 and prtP mutant K1. Mice were injected with live T. denticola ATCC 35405 (open bars) or mutant K1 (hatched bars), and lesion areas were determined at the indicated times following infection.
    Figure Legend Snippet: Mean areas of lesions at infection sites after challenge with T. denticola ATCC 35405 and prtP mutant K1. Mice were injected with live T. denticola ATCC 35405 (open bars) or mutant K1 (hatched bars), and lesion areas were determined at the indicated times following infection.

    Techniques Used: Infection, Mutagenesis, Mouse Assay, Injection

    Immunoblot analysis of T. denticola ATCC 35405 and K1 with anti- T. denticola ATCC 35405 whole-cell serum. Samples from lanes 1 to 4 were treated with PMSF. Lanes 1 and 5, T. denticola ATCC 35405 (without boiling); lanes 2 and 6, T. denticola K1 (without boiling); lanes 3 and 7, T. denticola ATCC 35405 (with boiling); lanes 4 and 8, T. denticola K1 (with boiling). Arrowheads indicate the high-molecular-mass oligomeric protein and the Msp band.
    Figure Legend Snippet: Immunoblot analysis of T. denticola ATCC 35405 and K1 with anti- T. denticola ATCC 35405 whole-cell serum. Samples from lanes 1 to 4 were treated with PMSF. Lanes 1 and 5, T. denticola ATCC 35405 (without boiling); lanes 2 and 6, T. denticola K1 (without boiling); lanes 3 and 7, T. denticola ATCC 35405 (with boiling); lanes 4 and 8, T. denticola K1 (with boiling). Arrowheads indicate the high-molecular-mass oligomeric protein and the Msp band.

    Techniques Used:

    Southern blot analysis of T. denticola ATCC 35405 and prtP mutant K1. Chromosomal DNAs from T. denticola ATCC 35405 (lanes 1 and 3) and prtP mutant K1 (lanes 2 and 4) were digested with Hin dIII and hybridized with a digoxigenin-labeled Kpn I- Pst I fragment from the prtP gene (lanes 1 and 2) or the Kpn I- Bam HI fragment from pVA2198 (lanes 3 and 4). Numbers at right are kilobase pairs.
    Figure Legend Snippet: Southern blot analysis of T. denticola ATCC 35405 and prtP mutant K1. Chromosomal DNAs from T. denticola ATCC 35405 (lanes 1 and 3) and prtP mutant K1 (lanes 2 and 4) were digested with Hin dIII and hybridized with a digoxigenin-labeled Kpn I- Pst I fragment from the prtP gene (lanes 1 and 2) or the Kpn I- Bam HI fragment from pVA2198 (lanes 3 and 4). Numbers at right are kilobase pairs.

    Techniques Used: Southern Blot, Mutagenesis, Labeling

    Gelatin zymography of sonicates of T. denticola ATCC 35405 (lane 1) and K1 (lane 2).
    Figure Legend Snippet: Gelatin zymography of sonicates of T. denticola ATCC 35405 (lane 1) and K1 (lane 2).

    Techniques Used: Zymography

    SDS-PAGE analysis of sonicates of T. denticola ATCC 35405 and K1. Samples from lanes 1 to 4 were treated with PMSF. Lanes 1 and 5, T. denticola ATCC 35405 (without boiling); lanes 2 and 6, T. denticola K1 (without boiling); lanes 3 and 7, T. denticola ATCC 35405 (with boiling); lanes 4 and 8, T. denticola K1 (with boiling). After electrophoresis, the gel was stained with Coomassie brilliant blue R-250. Arrowheads indicate the high-molecular-mass oligomeric protein and the Msp band.
    Figure Legend Snippet: SDS-PAGE analysis of sonicates of T. denticola ATCC 35405 and K1. Samples from lanes 1 to 4 were treated with PMSF. Lanes 1 and 5, T. denticola ATCC 35405 (without boiling); lanes 2 and 6, T. denticola K1 (without boiling); lanes 3 and 7, T. denticola ATCC 35405 (with boiling); lanes 4 and 8, T. denticola K1 (with boiling). After electrophoresis, the gel was stained with Coomassie brilliant blue R-250. Arrowheads indicate the high-molecular-mass oligomeric protein and the Msp band.

    Techniques Used: SDS Page, Electrophoresis, Staining

    Immunoblot analysis of T. denticola ATCC 35405 (lane 1; boiled) and K1 (lane 2; boiled) with antidentilisin serum.
    Figure Legend Snippet: Immunoblot analysis of T. denticola ATCC 35405 (lane 1; boiled) and K1 (lane 2; boiled) with antidentilisin serum.

    Techniques Used:

    48) Product Images from "Filamentous Actin Disruption and Diminished Inositol Phosphate Response in Gingival Fibroblasts Caused by Treponema denticola"

    Article Title: Filamentous Actin Disruption and Diminished Inositol Phosphate Response in Gingival Fibroblasts Caused by Treponema denticola

    Journal: Infection and Immunity

    doi:

    Histogram of fluorescence intensity of rhodamine-phalloidin-labeled F-actin in HGF during a 140-min time course, analyzed by confocal microscopy. There was significant depolymerization of F-actin in the T. denticola ATCC 35405-challenged HGF (left graph) in comparison with the control HGF (right graph). The degree of diminished fluorescence in T. denticola -challenged cells was significant at 60 min ( P
    Figure Legend Snippet: Histogram of fluorescence intensity of rhodamine-phalloidin-labeled F-actin in HGF during a 140-min time course, analyzed by confocal microscopy. There was significant depolymerization of F-actin in the T. denticola ATCC 35405-challenged HGF (left graph) in comparison with the control HGF (right graph). The degree of diminished fluorescence in T. denticola -challenged cells was significant at 60 min ( P

    Techniques Used: Fluorescence, Labeling, Confocal Microscopy

    Comparison of filamentous actin disruption (mean ± standard deviation) in HGF challenged with different concentrations of whole cells of T. denticola ATCC 35405 (□) and OM extract (▪). The dry weight for the OM and the dry weight for the T. denticola cells were equivalent at each optical density (OD) point shown on the x axis.
    Figure Legend Snippet: Comparison of filamentous actin disruption (mean ± standard deviation) in HGF challenged with different concentrations of whole cells of T. denticola ATCC 35405 (□) and OM extract (▪). The dry weight for the OM and the dry weight for the T. denticola cells were equivalent at each optical density (OD) point shown on the x axis.

    Techniques Used: Standard Deviation

    Qualitative comparison by SDS-PAGE of T. denticola ATCC 35405 whole cells (lane 1), OM extract run at the same time (lane 2), and repeat of the OM extract run in a different gel to resolve mid-range bands more clearly (lane 3). The positions of molecular size standards (broad-range SDS-PAGE standards; Bio-Rad) are shown in kilodaltons at the left. Conditions were as follows: Washed T. denticola suspensions (optical density of 1.2 at 550 nm) from 3-day cultures or undiluted OM extract were mixed 1:1 with sample buffer (0.25 M Tris-HCl [pH 6.8], 20% glycerol, 4.6% SDS, 0.02% bromophenol blue, 10% β-mercaptoethanol) and boiled for 10 min; 25 μl was added to each lane of a 1-mm-thick Ready Gel (Bio-Rad) with a 4% stacking gel and 12% resolving gel. Electrophoresis was run in a Mini-Protean II cell (Bio-Rad). Whole cells and OM extract had several bands in common.
    Figure Legend Snippet: Qualitative comparison by SDS-PAGE of T. denticola ATCC 35405 whole cells (lane 1), OM extract run at the same time (lane 2), and repeat of the OM extract run in a different gel to resolve mid-range bands more clearly (lane 3). The positions of molecular size standards (broad-range SDS-PAGE standards; Bio-Rad) are shown in kilodaltons at the left. Conditions were as follows: Washed T. denticola suspensions (optical density of 1.2 at 550 nm) from 3-day cultures or undiluted OM extract were mixed 1:1 with sample buffer (0.25 M Tris-HCl [pH 6.8], 20% glycerol, 4.6% SDS, 0.02% bromophenol blue, 10% β-mercaptoethanol) and boiled for 10 min; 25 μl was added to each lane of a 1-mm-thick Ready Gel (Bio-Rad) with a 4% stacking gel and 12% resolving gel. Electrophoresis was run in a Mini-Protean II cell (Bio-Rad). Whole cells and OM extract had several bands in common.

    Techniques Used: SDS Page, Nucleic Acid Electrophoresis

    49) Product Images from "Characterization of a potential ABC-type bacteriocin exporter protein from Treponema denticola"

    Article Title: Characterization of a potential ABC-type bacteriocin exporter protein from Treponema denticola

    Journal: BMC Oral Health

    doi: 10.1186/s12903-016-0243-7

    Southern blot analysis of tepA1 ( a ), tepA2 ( b ) , and tepA3 ( c ). Genomic DNA from T. denticola strains was digested with Hin dIII. 1: genomic DNA from ATCC 33520, 2: genomic DNA from ATCC 33521, genomic DNA from ATCC 35404, 4: genomic DNA from ATCC 35405, 5: genomic DNA from GM1
    Figure Legend Snippet: Southern blot analysis of tepA1 ( a ), tepA2 ( b ) , and tepA3 ( c ). Genomic DNA from T. denticola strains was digested with Hin dIII. 1: genomic DNA from ATCC 33520, 2: genomic DNA from ATCC 33521, genomic DNA from ATCC 35404, 4: genomic DNA from ATCC 35405, 5: genomic DNA from GM1

    Techniques Used: Southern Blot

    50) Product Images from "Characterization of a potential ABC-type bacteriocin exporter protein from Treponema denticola"

    Article Title: Characterization of a potential ABC-type bacteriocin exporter protein from Treponema denticola

    Journal: BMC Oral Health

    doi: 10.1186/s12903-016-0243-7

    Southern blot analysis of tepA1 ( a ), tepA2 ( b ) , and tepA3 ( c ). Genomic DNA from T. denticola strains was digested with Hin dIII. 1: genomic DNA from ATCC 33520, 2: genomic DNA from ATCC 33521, genomic DNA from ATCC 35404, 4: genomic DNA from ATCC 35405, 5: genomic DNA from GM1
    Figure Legend Snippet: Southern blot analysis of tepA1 ( a ), tepA2 ( b ) , and tepA3 ( c ). Genomic DNA from T. denticola strains was digested with Hin dIII. 1: genomic DNA from ATCC 33520, 2: genomic DNA from ATCC 33521, genomic DNA from ATCC 35404, 4: genomic DNA from ATCC 35405, 5: genomic DNA from GM1

    Techniques Used: Southern Blot

    51) Product Images from "The Chymotrypsin-Like Protease Complex of Treponema denticola ATCC 35405 Mediates Fibrinogen Adherence and Degradation ▿"

    Article Title: The Chymotrypsin-Like Protease Complex of Treponema denticola ATCC 35405 Mediates Fibrinogen Adherence and Degradation ▿

    Journal: Infection and Immunity

    doi: 10.1128/IAI.00258-07

    TCT in the absence or presence of T. denticola ATCC 35405, MHE (Msp − ), or CKE (CTLP − ). Human plasma was incubated with T. denticola (1.2 × 10 9 cells/ml) suspended in PBS or with PBS alone (control) for 5 min before the addition
    Figure Legend Snippet: TCT in the absence or presence of T. denticola ATCC 35405, MHE (Msp − ), or CKE (CTLP − ). Human plasma was incubated with T. denticola (1.2 × 10 9 cells/ml) suspended in PBS or with PBS alone (control) for 5 min before the addition

    Techniques Used: Incubation

    Fibrinogen zymograms of outer membrane proteins from T. denticola ATCC 35405, MHE (Msp − ), and CKE (CTLP − ). Triton X-114 extracts were incubated for 5 min at 20°C (−) or 100°C (+) before being subjected to
    Figure Legend Snippet: Fibrinogen zymograms of outer membrane proteins from T. denticola ATCC 35405, MHE (Msp − ), and CKE (CTLP − ). Triton X-114 extracts were incubated for 5 min at 20°C (−) or 100°C (+) before being subjected to

    Techniques Used: Incubation

    Purification and enzymatic activity of major fibrinogen-binding protein from T. denticola ATCC 35405. Outer membrane proteins were extracted with 0.1% Triton X-114 solution and incubated with fibrinogen-linked Sepharose, and then tightly bound
    Figure Legend Snippet: Purification and enzymatic activity of major fibrinogen-binding protein from T. denticola ATCC 35405. Outer membrane proteins were extracted with 0.1% Triton X-114 solution and incubated with fibrinogen-linked Sepharose, and then tightly bound

    Techniques Used: Purification, Activity Assay, Binding Assay, Incubation

    Binding of fluid-phase or immobilized fibrinogen by T. denticola ATCC 35405 (⧫), MHE (Msp − ; ▴), or CKE (CTLP − ; ▪). (A and B) Treponema cells immobilized onto plastic wells in the absence (A) or presence (B) of 0.05
    Figure Legend Snippet: Binding of fluid-phase or immobilized fibrinogen by T. denticola ATCC 35405 (⧫), MHE (Msp − ; ▴), or CKE (CTLP − ; ▪). (A and B) Treponema cells immobilized onto plastic wells in the absence (A) or presence (B) of 0.05

    Techniques Used: Binding Assay

    Fibrinogen blot overlay of outer membrane protein extracts from T. denticola ATCC 35405, MHE, and CKE. Proteins were extracted with 1% Triton X-114 and incubated for 5 min at 20°C (−) or 100°C (+) before being subjected
    Figure Legend Snippet: Fibrinogen blot overlay of outer membrane protein extracts from T. denticola ATCC 35405, MHE, and CKE. Proteins were extracted with 1% Triton X-114 and incubated for 5 min at 20°C (−) or 100°C (+) before being subjected

    Techniques Used: Incubation

    Adherence of T. denticola ATCC 35405 cells to denatured fibrinogen or recombinant fibrinogen polypeptides. (A) Human fibrinogen (N) or purified recombinant Aα, Bβ, and γ chain polypeptides were heated for 5 min at 100°C
    Figure Legend Snippet: Adherence of T. denticola ATCC 35405 cells to denatured fibrinogen or recombinant fibrinogen polypeptides. (A) Human fibrinogen (N) or purified recombinant Aα, Bβ, and γ chain polypeptides were heated for 5 min at 100°C

    Techniques Used: Recombinant, Purification

    52) Product Images from "The Chymotrypsin-Like Protease Complex of Treponema denticola ATCC 35405 Mediates Fibrinogen Adherence and Degradation ▿"

    Article Title: The Chymotrypsin-Like Protease Complex of Treponema denticola ATCC 35405 Mediates Fibrinogen Adherence and Degradation ▿

    Journal: Infection and Immunity

    doi: 10.1128/IAI.00258-07

    TCT in the absence or presence of T. denticola ATCC 35405, MHE (Msp − ), or CKE (CTLP − ). Human plasma was incubated with T. denticola (1.2 × 10 9 cells/ml) suspended in PBS or with PBS alone (control) for 5 min before the addition
    Figure Legend Snippet: TCT in the absence or presence of T. denticola ATCC 35405, MHE (Msp − ), or CKE (CTLP − ). Human plasma was incubated with T. denticola (1.2 × 10 9 cells/ml) suspended in PBS or with PBS alone (control) for 5 min before the addition

    Techniques Used: Incubation

    Fibrinogen zymograms of outer membrane proteins from T. denticola ATCC 35405, MHE (Msp − ), and CKE (CTLP − ). Triton X-114 extracts were incubated for 5 min at 20°C (−) or 100°C (+) before being subjected to
    Figure Legend Snippet: Fibrinogen zymograms of outer membrane proteins from T. denticola ATCC 35405, MHE (Msp − ), and CKE (CTLP − ). Triton X-114 extracts were incubated for 5 min at 20°C (−) or 100°C (+) before being subjected to

    Techniques Used: Incubation

    Purification and enzymatic activity of major fibrinogen-binding protein from T. denticola ATCC 35405. Outer membrane proteins were extracted with 0.1% Triton X-114 solution and incubated with fibrinogen-linked Sepharose, and then tightly bound
    Figure Legend Snippet: Purification and enzymatic activity of major fibrinogen-binding protein from T. denticola ATCC 35405. Outer membrane proteins were extracted with 0.1% Triton X-114 solution and incubated with fibrinogen-linked Sepharose, and then tightly bound

    Techniques Used: Purification, Activity Assay, Binding Assay, Incubation

    Binding of fluid-phase or immobilized fibrinogen by T. denticola ATCC 35405 (⧫), MHE (Msp − ; ▴), or CKE (CTLP − ; ▪). (A and B) Treponema cells immobilized onto plastic wells in the absence (A) or presence (B) of 0.05
    Figure Legend Snippet: Binding of fluid-phase or immobilized fibrinogen by T. denticola ATCC 35405 (⧫), MHE (Msp − ; ▴), or CKE (CTLP − ; ▪). (A and B) Treponema cells immobilized onto plastic wells in the absence (A) or presence (B) of 0.05

    Techniques Used: Binding Assay

    Fibrinogen blot overlay of outer membrane protein extracts from T. denticola ATCC 35405, MHE, and CKE. Proteins were extracted with 1% Triton X-114 and incubated for 5 min at 20°C (−) or 100°C (+) before being subjected
    Figure Legend Snippet: Fibrinogen blot overlay of outer membrane protein extracts from T. denticola ATCC 35405, MHE, and CKE. Proteins were extracted with 1% Triton X-114 and incubated for 5 min at 20°C (−) or 100°C (+) before being subjected

    Techniques Used: Incubation

    Adherence of T. denticola ATCC 35405 cells to denatured fibrinogen or recombinant fibrinogen polypeptides. (A) Human fibrinogen (N) or purified recombinant Aα, Bβ, and γ chain polypeptides were heated for 5 min at 100°C
    Figure Legend Snippet: Adherence of T. denticola ATCC 35405 cells to denatured fibrinogen or recombinant fibrinogen polypeptides. (A) Human fibrinogen (N) or purified recombinant Aα, Bβ, and γ chain polypeptides were heated for 5 min at 100°C

    Techniques Used: Recombinant, Purification

    53) Product Images from "Genome-Wide Relatedness of Treponema pedis, from Gingiva and Necrotic Skin Lesions of Pigs, with the Human Oral Pathogen Treponema denticola"

    Article Title: Genome-Wide Relatedness of Treponema pedis, from Gingiva and Necrotic Skin Lesions of Pigs, with the Human Oral Pathogen Treponema denticola

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0071281

    Circular representation of the T. pedis T A4 genome and complete genome alignment with T. denticola . (A.) Circular representation of the T. pedis T A4 genome. The CDSs are shown in violet where the outer circle represents predictions on the plus strand and the second circle those on the minus strand. CDSs with a best BLASTP hit in T. denticola ATCC 35405 are colored red and shown in the third circle. The fourth circle represents genes with best BLASTP hits in T. brennaborense (black), F. nucleatum (green), F. alocis (blue) and T. succinifaciens (grey). G+C skew is drawn in the inner circle. (B.) Complete genome alignment between T. pedis T A4 and T. denticola ATCC 35405. Dots represent maximum unique matches (MUMs) between the genomes. MUMs oriented in the same direction are depicted as red dots and reverse complemented MUMs are depicted as blue dots.
    Figure Legend Snippet: Circular representation of the T. pedis T A4 genome and complete genome alignment with T. denticola . (A.) Circular representation of the T. pedis T A4 genome. The CDSs are shown in violet where the outer circle represents predictions on the plus strand and the second circle those on the minus strand. CDSs with a best BLASTP hit in T. denticola ATCC 35405 are colored red and shown in the third circle. The fourth circle represents genes with best BLASTP hits in T. brennaborense (black), F. nucleatum (green), F. alocis (blue) and T. succinifaciens (grey). G+C skew is drawn in the inner circle. (B.) Complete genome alignment between T. pedis T A4 and T. denticola ATCC 35405. Dots represent maximum unique matches (MUMs) between the genomes. MUMs oriented in the same direction are depicted as red dots and reverse complemented MUMs are depicted as blue dots.

    Techniques Used:

    54) Product Images from "Genome-Wide Relatedness of Treponema pedis, from Gingiva and Necrotic Skin Lesions of Pigs, with the Human Oral Pathogen Treponema denticola"

    Article Title: Genome-Wide Relatedness of Treponema pedis, from Gingiva and Necrotic Skin Lesions of Pigs, with the Human Oral Pathogen Treponema denticola

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0071281

    Circular representation of the T. pedis T A4 genome and complete genome alignment with T. denticola . (A.) Circular representation of the T. pedis T A4 genome. The CDSs are shown in violet where the outer circle represents predictions on the plus strand and the second circle those on the minus strand. CDSs with a best BLASTP hit in T. denticola ATCC 35405 are colored red and shown in the third circle. The fourth circle represents genes with best BLASTP hits in T. brennaborense (black), F. nucleatum (green), F. alocis (blue) and T. succinifaciens (grey). G+C skew is drawn in the inner circle. (B.) Complete genome alignment between T. pedis T A4 and T. denticola ATCC 35405. Dots represent maximum unique matches (MUMs) between the genomes. MUMs oriented in the same direction are depicted as red dots and reverse complemented MUMs are depicted as blue dots.
    Figure Legend Snippet: Circular representation of the T. pedis T A4 genome and complete genome alignment with T. denticola . (A.) Circular representation of the T. pedis T A4 genome. The CDSs are shown in violet where the outer circle represents predictions on the plus strand and the second circle those on the minus strand. CDSs with a best BLASTP hit in T. denticola ATCC 35405 are colored red and shown in the third circle. The fourth circle represents genes with best BLASTP hits in T. brennaborense (black), F. nucleatum (green), F. alocis (blue) and T. succinifaciens (grey). G+C skew is drawn in the inner circle. (B.) Complete genome alignment between T. pedis T A4 and T. denticola ATCC 35405. Dots represent maximum unique matches (MUMs) between the genomes. MUMs oriented in the same direction are depicted as red dots and reverse complemented MUMs are depicted as blue dots.

    Techniques Used:

    55) Product Images from "Genome-Wide Relatedness of Treponema pedis, from Gingiva and Necrotic Skin Lesions of Pigs, with the Human Oral Pathogen Treponema denticola"

    Article Title: Genome-Wide Relatedness of Treponema pedis, from Gingiva and Necrotic Skin Lesions of Pigs, with the Human Oral Pathogen Treponema denticola

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0071281

    Circular representation of the T. pedis T A4 genome and complete genome alignment with T. denticola . (A.) Circular representation of the T. pedis T A4 genome. The CDSs are shown in violet where the outer circle represents predictions on the plus strand and the second circle those on the minus strand. CDSs with a best BLASTP hit in T. denticola ATCC 35405 are colored red and shown in the third circle. The fourth circle represents genes with best BLASTP hits in T. brennaborense (black), F. nucleatum (green), F. alocis (blue) and T. succinifaciens (grey). G+C skew is drawn in the inner circle. (B.) Complete genome alignment between T. pedis T A4 and T. denticola ATCC 35405. Dots represent maximum unique matches (MUMs) between the genomes. MUMs oriented in the same direction are depicted as red dots and reverse complemented MUMs are depicted as blue dots.
    Figure Legend Snippet: Circular representation of the T. pedis T A4 genome and complete genome alignment with T. denticola . (A.) Circular representation of the T. pedis T A4 genome. The CDSs are shown in violet where the outer circle represents predictions on the plus strand and the second circle those on the minus strand. CDSs with a best BLASTP hit in T. denticola ATCC 35405 are colored red and shown in the third circle. The fourth circle represents genes with best BLASTP hits in T. brennaborense (black), F. nucleatum (green), F. alocis (blue) and T. succinifaciens (grey). G+C skew is drawn in the inner circle. (B.) Complete genome alignment between T. pedis T A4 and T. denticola ATCC 35405. Dots represent maximum unique matches (MUMs) between the genomes. MUMs oriented in the same direction are depicted as red dots and reverse complemented MUMs are depicted as blue dots.

    Techniques Used:

    56) Product Images from "Characterization of a novel family of fibronectin-binding proteins with M23 peptidase domains from Treponema denticola"

    Article Title: Characterization of a novel family of fibronectin-binding proteins with M23 peptidase domains from Treponema denticola

    Journal: Molecular oral microbiology

    doi: 10.1111/j.2041-1014.2010.00584.x

    Detection of proteins on the surface of Treponema denticola ATCC 35405 using antibodies to the Treponema pallidum protein Tp0155 which had first been pre-adsorbed against Treponema phagedenis (Kazan). (A, C, E, G, I, K and M) Phase-contrast images; (B, D, F, H, J, L and N) corresponding immunofluorescence. (A, B) Preimmune serum for Tp0155-specific antibodies; (C, D), Tp0155-specific antibodies, non-detergent-treated T. denticola ; (E, F), Tp0155-specific antibodies, Triton X-114-treated T. denticola ; (G, H), preimmune serum for Tp0249-specific antibodies; (I, J), Tp0249-specific antibodies, non-detergent-treated T. denticola (negative control); (K, L), Tp0249-specific antibodies, Triton X-114-treated T. denticola ; (M, N), anti- T. denticola ).
    Figure Legend Snippet: Detection of proteins on the surface of Treponema denticola ATCC 35405 using antibodies to the Treponema pallidum protein Tp0155 which had first been pre-adsorbed against Treponema phagedenis (Kazan). (A, C, E, G, I, K and M) Phase-contrast images; (B, D, F, H, J, L and N) corresponding immunofluorescence. (A, B) Preimmune serum for Tp0155-specific antibodies; (C, D), Tp0155-specific antibodies, non-detergent-treated T. denticola ; (E, F), Tp0155-specific antibodies, Triton X-114-treated T. denticola ; (G, H), preimmune serum for Tp0249-specific antibodies; (I, J), Tp0249-specific antibodies, non-detergent-treated T. denticola (negative control); (K, L), Tp0249-specific antibodies, Triton X-114-treated T. denticola ; (M, N), anti- T. denticola ).

    Techniques Used: Immunofluorescence, Negative Control

    57) Product Images from "Identification of a Treponema denticola OppA Homologue That Binds Host Proteins Present in the Subgingival Environment"

    Article Title: Identification of a Treponema denticola OppA Homologue That Binds Host Proteins Present in the Subgingival Environment

    Journal: Infection and Immunity

    doi:

    Binding of soluble host proteins to T. denticola cells and proteins. (A) ELISA format. FN, plasminogen (Pgn), or BSA in PBS were added to wells containing immobilized T. denticola ATCC 35405 cells (T.d.), native OppA (OppA), recombinant LacZ-OppA fusion protein (rOppA40), recombinant Msp (rMsp), or BSA. Bound FN and plasminogen were detected with anti-FN (shaded bars) and anti-plasminogen (hatched bars) antibodies, respectively. The y axis shows absorbance at 405 nm. Data shown represent the means ± standard deviations of at least two experiments using triplicate samples. (B) Ligand blot format. Duplicate samples of protein (1 μg) or cells (0.1 ml, OD 600 = 0.2) applied to nitrocellulose membranes were probed with plasminogen (samples 2 to 4) or plasminogen plus EACA (sample 5). Bound plasminogen was detected with anti-plasminogen immunoglobulin G. Lanes: 1, Plasminogen; 2, 5, and 6, T. denticola ATCC 35405; 3, T. denticola OHE; 4, T. denticola MHE.
    Figure Legend Snippet: Binding of soluble host proteins to T. denticola cells and proteins. (A) ELISA format. FN, plasminogen (Pgn), or BSA in PBS were added to wells containing immobilized T. denticola ATCC 35405 cells (T.d.), native OppA (OppA), recombinant LacZ-OppA fusion protein (rOppA40), recombinant Msp (rMsp), or BSA. Bound FN and plasminogen were detected with anti-FN (shaded bars) and anti-plasminogen (hatched bars) antibodies, respectively. The y axis shows absorbance at 405 nm. Data shown represent the means ± standard deviations of at least two experiments using triplicate samples. (B) Ligand blot format. Duplicate samples of protein (1 μg) or cells (0.1 ml, OD 600 = 0.2) applied to nitrocellulose membranes were probed with plasminogen (samples 2 to 4) or plasminogen plus EACA (sample 5). Bound plasminogen was detected with anti-plasminogen immunoglobulin G. Lanes: 1, Plasminogen; 2, 5, and 6, T. denticola ATCC 35405; 3, T. denticola OHE; 4, T. denticola MHE.

    Techniques Used: Binding Assay, Enzyme-linked Immunosorbent Assay, Recombinant

    Confirmation of construction of allelic replacement mutants in the opp locus. (A) Southern blots of Sca I-digested T. denticola genomic DNA were probed with a biotinylated internal oppA fragment ( opp ) and the 2.1-kb ermF/AM cassette ( erm ). The ermF/AM cassette contains a single Sca I site. (B) Western immunoblot of T. denticola lysates probed with anti-70 antibodies. Lanes: 1, parent strain ATCC 35405; 2, oppA mutant strain OHE; 3, oppF mutant strain OXE.
    Figure Legend Snippet: Confirmation of construction of allelic replacement mutants in the opp locus. (A) Southern blots of Sca I-digested T. denticola genomic DNA were probed with a biotinylated internal oppA fragment ( opp ) and the 2.1-kb ermF/AM cassette ( erm ). The ermF/AM cassette contains a single Sca I site. (B) Western immunoblot of T. denticola lysates probed with anti-70 antibodies. Lanes: 1, parent strain ATCC 35405; 2, oppA mutant strain OHE; 3, oppF mutant strain OXE.

    Techniques Used: Western Blot, Mutagenesis

    Conservation of oppA in oral Treponema strains. (A) Southern blot of Hin dIII-digested chromosomal DNA probed with a 0.9-kb internal fragment of oppA . (B) Western blot of whole-cell extracts probed with anti-40 antibodies. Lanes: 1, T. denticola ATCC 35405; 2, T. denticola ATCC 35404; 3, T. denticola ATCC 33520; 4, T. vincentii LA-1; 5, T. denticola OTK; 6, T. denticola GM-1; 7, T. socranskii ATCC 35536; 8, T. pectinovorum ATCC 33768.
    Figure Legend Snippet: Conservation of oppA in oral Treponema strains. (A) Southern blot of Hin dIII-digested chromosomal DNA probed with a 0.9-kb internal fragment of oppA . (B) Western blot of whole-cell extracts probed with anti-40 antibodies. Lanes: 1, T. denticola ATCC 35405; 2, T. denticola ATCC 35404; 3, T. denticola ATCC 33520; 4, T. vincentii LA-1; 5, T. denticola OTK; 6, T. denticola GM-1; 7, T. socranskii ATCC 35536; 8, T. pectinovorum ATCC 33768.

    Techniques Used: Southern Blot, Western Blot

    58) Product Images from "Disruption of a Type II Endonuclease (TDE0911) Enables Treponema denticola ATCC 35405 To Accept an Unmethylated Shuttle Vector ▿"

    Article Title: Disruption of a Type II Endonuclease (TDE0911) Enables Treponema denticola ATCC 35405 To Accept an Unmethylated Shuttle Vector ▿

    Journal: Applied and Environmental Microbiology

    doi: 10.1128/AEM.00417-11

    Transformation of pBFC into different T. denticola strains. Ten micrograms of methylated (mpBFC, top panels) or unmethylated pBFC plasmid (umpBFC, bottom panels) was electroporated into ATCC 35405, ATCC 33520, and the TdΔ911 mutant. Images were
    Figure Legend Snippet: Transformation of pBFC into different T. denticola strains. Ten micrograms of methylated (mpBFC, top panels) or unmethylated pBFC plasmid (umpBFC, bottom panels) was electroporated into ATCC 35405, ATCC 33520, and the TdΔ911 mutant. Images were

    Techniques Used: Transformation Assay, Methylation, Plasmid Preparation, Mutagenesis

    59) Product Images from "Disruption of a Type II Endonuclease (TDE0911) Enables Treponema denticola ATCC 35405 To Accept an Unmethylated Shuttle Vector ▿"

    Article Title: Disruption of a Type II Endonuclease (TDE0911) Enables Treponema denticola ATCC 35405 To Accept an Unmethylated Shuttle Vector ▿

    Journal: Applied and Environmental Microbiology

    doi: 10.1128/AEM.00417-11

    Transformation of pBFC into different T. denticola strains. Ten micrograms of methylated (mpBFC, top panels) or unmethylated pBFC plasmid (umpBFC, bottom panels) was electroporated into ATCC 35405, ATCC 33520, and the TdΔ911 mutant. Images were
    Figure Legend Snippet: Transformation of pBFC into different T. denticola strains. Ten micrograms of methylated (mpBFC, top panels) or unmethylated pBFC plasmid (umpBFC, bottom panels) was electroporated into ATCC 35405, ATCC 33520, and the TdΔ911 mutant. Images were

    Techniques Used: Transformation Assay, Methylation, Plasmid Preparation, Mutagenesis

    60) Product Images from "Treponema denticola chymotrypsin-like proteinase (CTLP) integrates spirochaetes within oral microbial communities"

    Article Title: Treponema denticola chymotrypsin-like proteinase (CTLP) integrates spirochaetes within oral microbial communities

    Journal: Microbiology

    doi: 10.1099/mic.0.055939-0

    Role of the CTLP complex in the formation of T. denticola / P. gingivalis dual-species biofilms. Representative CLSM images of dual-species biofilms of (a, b) T. denticola ATCC 35405 and (c, d) T. denticola CKE, with P. gingivalis ATCC 33277. Biofilms were
    Figure Legend Snippet: Role of the CTLP complex in the formation of T. denticola / P. gingivalis dual-species biofilms. Representative CLSM images of dual-species biofilms of (a, b) T. denticola ATCC 35405 and (c, d) T. denticola CKE, with P. gingivalis ATCC 33277. Biofilms were

    Techniques Used: Confocal Laser Scanning Microscopy

    Adherence levels of Treponema to other periodontopathogens. The input cell number was 1.2×10 7 cells per well of T. denticola ATCC 35405 (black bars), T. denticola MHE (mid-grey bars), T. denticola CKE (dark-grey bars) and T. vincentii ATCC 35580
    Figure Legend Snippet: Adherence levels of Treponema to other periodontopathogens. The input cell number was 1.2×10 7 cells per well of T. denticola ATCC 35405 (black bars), T. denticola MHE (mid-grey bars), T. denticola CKE (dark-grey bars) and T. vincentii ATCC 35580

    Techniques Used:

    Fluorescence microscopy of monospecies or dual-species biofilms of T. denticola ATCC 35405, T. denticola CKE or T. denticola MHE, and P. gingivalis ATCC 33277, and corresponding biomass data. (a) Biofilms formed upon saliva-coated coverslips after 72
    Figure Legend Snippet: Fluorescence microscopy of monospecies or dual-species biofilms of T. denticola ATCC 35405, T. denticola CKE or T. denticola MHE, and P. gingivalis ATCC 33277, and corresponding biomass data. (a) Biofilms formed upon saliva-coated coverslips after 72

    Techniques Used: Fluorescence, Microscopy

    61) Product Images from "Dentipain, a Streptococcus-pyogenes-IdeS-protease homologue, is a novel virulence factor of Treponema denticola"

    Article Title: Dentipain, a Streptococcus-pyogenes-IdeS-protease homologue, is a novel virulence factor of Treponema denticola

    Journal: Biological chemistry

    doi: 10.1515/BC.2010.113

    Construction of an IdeT protease-deficient mutant A . (i) The wild-type ideT locus detailing the four protein domains; (ii) pIDEKO4, constructed using pMCL191, two ideT PCR generated fragments flanking the proteolytic domain (hatched bar and dotted bar) and an erythromycin resistance cassette derived from pVA2198. The restriction sites introduced during PCR are also shown; (iii) the ideT mutant locus detailing the dentipain region replaced with an erythromycin resistance cassette by homologous recombination. B . (i) PCR amplification of the ideT locus using primers ID-1 and ID-4, which amplify from amino acid residues 172 to 640. Lane 1, T. denticola ATCC 35405; lane 2, T. denticola IDEKO4; lane 3, T. denticola Ide5; lane 4, T. denticola Ide6; lane 5 , Molecular size marker. (ii) PCR amplification of the ideT locus using primers ID-1 and CATU, which amplify from amino acid residues 172 to 417. Lane 1, T. denticola ATCC 35405; lane 2, T. denticola IDEKO4; lane 3 , Molecular size marker.
    Figure Legend Snippet: Construction of an IdeT protease-deficient mutant A . (i) The wild-type ideT locus detailing the four protein domains; (ii) pIDEKO4, constructed using pMCL191, two ideT PCR generated fragments flanking the proteolytic domain (hatched bar and dotted bar) and an erythromycin resistance cassette derived from pVA2198. The restriction sites introduced during PCR are also shown; (iii) the ideT mutant locus detailing the dentipain region replaced with an erythromycin resistance cassette by homologous recombination. B . (i) PCR amplification of the ideT locus using primers ID-1 and ID-4, which amplify from amino acid residues 172 to 640. Lane 1, T. denticola ATCC 35405; lane 2, T. denticola IDEKO4; lane 3, T. denticola Ide5; lane 4, T. denticola Ide6; lane 5 , Molecular size marker. (ii) PCR amplification of the ideT locus using primers ID-1 and CATU, which amplify from amino acid residues 172 to 417. Lane 1, T. denticola ATCC 35405; lane 2, T. denticola IDEKO4; lane 3 , Molecular size marker.

    Techniques Used: Mutagenesis, Construct, Polymerase Chain Reaction, Generated, Derivative Assay, Homologous Recombination, Amplification, Marker

    Analysis of IdeT translation A. SDS-PAGE of T. denticola sonicates. Lane 1, T. denticola ATCC 35405 sonicate; lane 2, T. denticola IDEKO4 sonicate. B. Immunoblot analysis of IdeT from T. denticola cells. Lane 1, T. denticola ATCC 35405 sonicate; lane 2, T. denticola IDEKO4 sonicate. Antibody: rabbit serum anti-IdeT recombinant protein (219–647). The arrow indicates the band which reacted with this antibody. C. SDS-PAGE of concentrated culture supernatant of T. denticola . Culture supernatant of T. denticola grown in E-TYGV medium was collected and concentrated. Lane 1, culture supernatant of T. denticola ATCC 35405; lane 2, culture supernatant of T. denticola IDEKO4. D. Immunoblot analysis of IdeT in culture supernatants. Lane 1, culture supernatant of T. denticola ATCC 35405; lane 2, culture supernatant of T. denticola IDEKO4. Antibody: rabbit serum anti-IdeT recombinant protein (219–647). The arrow indicates the band which reacted with this antibody. E. Immunoblot analysis of IdeT in culture supernatants. Lane 1, culture supernatant of T. denticola ATCC 3540 5; lane 2, culture supernatant of T. denticola IDEK O4. Antibody : rabbit serum anti-IdeT synthetic peptide (IdeT498–511). The arrow indicates the band which reacted with this antibody.
    Figure Legend Snippet: Analysis of IdeT translation A. SDS-PAGE of T. denticola sonicates. Lane 1, T. denticola ATCC 35405 sonicate; lane 2, T. denticola IDEKO4 sonicate. B. Immunoblot analysis of IdeT from T. denticola cells. Lane 1, T. denticola ATCC 35405 sonicate; lane 2, T. denticola IDEKO4 sonicate. Antibody: rabbit serum anti-IdeT recombinant protein (219–647). The arrow indicates the band which reacted with this antibody. C. SDS-PAGE of concentrated culture supernatant of T. denticola . Culture supernatant of T. denticola grown in E-TYGV medium was collected and concentrated. Lane 1, culture supernatant of T. denticola ATCC 35405; lane 2, culture supernatant of T. denticola IDEKO4. D. Immunoblot analysis of IdeT in culture supernatants. Lane 1, culture supernatant of T. denticola ATCC 35405; lane 2, culture supernatant of T. denticola IDEKO4. Antibody: rabbit serum anti-IdeT recombinant protein (219–647). The arrow indicates the band which reacted with this antibody. E. Immunoblot analysis of IdeT in culture supernatants. Lane 1, culture supernatant of T. denticola ATCC 3540 5; lane 2, culture supernatant of T. denticola IDEK O4. Antibody : rabbit serum anti-IdeT synthetic peptide (IdeT498–511). The arrow indicates the band which reacted with this antibody.

    Techniques Used: SDS Page, Recombinant

    Analysis of the role of IdeT proteolytic activity in the virulence of T. denticola . Bars represent the mean area of lesions at the infection sites following challenge with either T. denticola ATCC 35405 or T. denticola IDEKO4. Mice were injected with live T. denticola ATCC 35405 (black bars) or IDEKO4 (open bars), and lesion areas determined at the indicated times following infection. Bars indicate standard deviation. *P
    Figure Legend Snippet: Analysis of the role of IdeT proteolytic activity in the virulence of T. denticola . Bars represent the mean area of lesions at the infection sites following challenge with either T. denticola ATCC 35405 or T. denticola IDEKO4. Mice were injected with live T. denticola ATCC 35405 (black bars) or IDEKO4 (open bars), and lesion areas determined at the indicated times following infection. Bars indicate standard deviation. *P

    Techniques Used: Activity Assay, Infection, Mouse Assay, Injection, Standard Deviation

    62) Product Images from "Dentilisin Activity Affects the Organization of the Outer Sheath of Treponema denticola"

    Article Title: Dentilisin Activity Affects the Organization of the Outer Sheath of Treponema denticola

    Journal: Journal of Bacteriology

    doi:

    Mean areas of lesions at infection sites after challenge with T. denticola ATCC 35405 and prtP mutant K1. Mice were injected with live T. denticola ATCC 35405 (open bars) or mutant K1 (hatched bars), and lesion areas were determined at the indicated times following infection.
    Figure Legend Snippet: Mean areas of lesions at infection sites after challenge with T. denticola ATCC 35405 and prtP mutant K1. Mice were injected with live T. denticola ATCC 35405 (open bars) or mutant K1 (hatched bars), and lesion areas were determined at the indicated times following infection.

    Techniques Used: Infection, Mutagenesis, Mouse Assay, Injection

    Immunoblot analysis of T. denticola ATCC 35405 and K1 with anti- T. denticola ATCC 35405 whole-cell serum. Samples from lanes 1 to 4 were treated with PMSF. Lanes 1 and 5, T. denticola ATCC 35405 (without boiling); lanes 2 and 6, T. denticola K1 (without boiling); lanes 3 and 7, T. denticola ATCC 35405 (with boiling); lanes 4 and 8, T. denticola K1 (with boiling). Arrowheads indicate the high-molecular-mass oligomeric protein and the Msp band.
    Figure Legend Snippet: Immunoblot analysis of T. denticola ATCC 35405 and K1 with anti- T. denticola ATCC 35405 whole-cell serum. Samples from lanes 1 to 4 were treated with PMSF. Lanes 1 and 5, T. denticola ATCC 35405 (without boiling); lanes 2 and 6, T. denticola K1 (without boiling); lanes 3 and 7, T. denticola ATCC 35405 (with boiling); lanes 4 and 8, T. denticola K1 (with boiling). Arrowheads indicate the high-molecular-mass oligomeric protein and the Msp band.

    Techniques Used:

    Southern blot analysis of T. denticola ATCC 35405 and prtP mutant K1. Chromosomal DNAs from T. denticola ATCC 35405 (lanes 1 and 3) and prtP mutant K1 (lanes 2 and 4) were digested with Hin dIII and hybridized with a digoxigenin-labeled Kpn I- Pst I fragment from the prtP gene (lanes 1 and 2) or the Kpn I- Bam HI fragment from pVA2198 (lanes 3 and 4). Numbers at right are kilobase pairs.
    Figure Legend Snippet: Southern blot analysis of T. denticola ATCC 35405 and prtP mutant K1. Chromosomal DNAs from T. denticola ATCC 35405 (lanes 1 and 3) and prtP mutant K1 (lanes 2 and 4) were digested with Hin dIII and hybridized with a digoxigenin-labeled Kpn I- Pst I fragment from the prtP gene (lanes 1 and 2) or the Kpn I- Bam HI fragment from pVA2198 (lanes 3 and 4). Numbers at right are kilobase pairs.

    Techniques Used: Southern Blot, Mutagenesis, Labeling

    Gelatin zymography of sonicates of T. denticola ATCC 35405 (lane 1) and K1 (lane 2).
    Figure Legend Snippet: Gelatin zymography of sonicates of T. denticola ATCC 35405 (lane 1) and K1 (lane 2).

    Techniques Used: Zymography

    SDS-PAGE analysis of sonicates of T. denticola ATCC 35405 and K1. Samples from lanes 1 to 4 were treated with PMSF. Lanes 1 and 5, T. denticola ATCC 35405 (without boiling); lanes 2 and 6, T. denticola K1 (without boiling); lanes 3 and 7, T. denticola ATCC 35405 (with boiling); lanes 4 and 8, T. denticola K1 (with boiling). After electrophoresis, the gel was stained with Coomassie brilliant blue R-250. Arrowheads indicate the high-molecular-mass oligomeric protein and the Msp band.
    Figure Legend Snippet: SDS-PAGE analysis of sonicates of T. denticola ATCC 35405 and K1. Samples from lanes 1 to 4 were treated with PMSF. Lanes 1 and 5, T. denticola ATCC 35405 (without boiling); lanes 2 and 6, T. denticola K1 (without boiling); lanes 3 and 7, T. denticola ATCC 35405 (with boiling); lanes 4 and 8, T. denticola K1 (with boiling). After electrophoresis, the gel was stained with Coomassie brilliant blue R-250. Arrowheads indicate the high-molecular-mass oligomeric protein and the Msp band.

    Techniques Used: SDS Page, Electrophoresis, Staining

    Immunoblot analysis of T. denticola ATCC 35405 (lane 1; boiled) and K1 (lane 2; boiled) with antidentilisin serum.
    Figure Legend Snippet: Immunoblot analysis of T. denticola ATCC 35405 (lane 1; boiled) and K1 (lane 2; boiled) with antidentilisin serum.

    Techniques Used:

    63) Product Images from "Cytopathic Effects of the Major Surface Protein and the Chymotrypsinlike Protease of Treponema denticola"

    Article Title: Cytopathic Effects of the Major Surface Protein and the Chymotrypsinlike Protease of Treponema denticola

    Journal: Infection and Immunity

    doi:

    Transmission electron micrograph of T. denticola ATCC 35405 outer membrane material released by mild sonication and probed with antibodies directed against Msp (10-nm gold beads) and CTLP (5-nm gold beads). Bar, 0.3 μm.
    Figure Legend Snippet: Transmission electron micrograph of T. denticola ATCC 35405 outer membrane material released by mild sonication and probed with antibodies directed against Msp (10-nm gold beads) and CTLP (5-nm gold beads). Bar, 0.3 μm.

    Techniques Used: Transmission Assay, Sonication

    64) Product Images from "Characterization of a potential ABC-type bacteriocin exporter protein from Treponema denticola"

    Article Title: Characterization of a potential ABC-type bacteriocin exporter protein from Treponema denticola

    Journal: BMC Oral Health

    doi: 10.1186/s12903-016-0243-7

    Southern blot analysis of tepA1 ( a ), tepA2 ( b ) , and tepA3 ( c ). Genomic DNA from T. denticola strains was digested with Hin dIII. 1: genomic DNA from ATCC 33520, 2: genomic DNA from ATCC 33521, genomic DNA from ATCC 35404, 4: genomic DNA from ATCC 35405, 5: genomic DNA from GM1
    Figure Legend Snippet: Southern blot analysis of tepA1 ( a ), tepA2 ( b ) , and tepA3 ( c ). Genomic DNA from T. denticola strains was digested with Hin dIII. 1: genomic DNA from ATCC 33520, 2: genomic DNA from ATCC 33521, genomic DNA from ATCC 35404, 4: genomic DNA from ATCC 35405, 5: genomic DNA from GM1

    Techniques Used: Southern Blot

    65) Product Images from "Characterization of a potential ABC-type bacteriocin exporter protein from Treponema denticola"

    Article Title: Characterization of a potential ABC-type bacteriocin exporter protein from Treponema denticola

    Journal: BMC Oral Health

    doi: 10.1186/s12903-016-0243-7

    Southern blot analysis of tepA1 ( a ), tepA2 ( b ) , and tepA3 ( c ). Genomic DNA from T. denticola strains was digested with Hin dIII. 1: genomic DNA from ATCC 33520, 2: genomic DNA from ATCC 33521, genomic DNA from ATCC 35404, 4: genomic DNA from ATCC 35405, 5: genomic DNA from GM1
    Figure Legend Snippet: Southern blot analysis of tepA1 ( a ), tepA2 ( b ) , and tepA3 ( c ). Genomic DNA from T. denticola strains was digested with Hin dIII. 1: genomic DNA from ATCC 33520, 2: genomic DNA from ATCC 33521, genomic DNA from ATCC 35404, 4: genomic DNA from ATCC 35405, 5: genomic DNA from GM1

    Techniques Used: Southern Blot

    66) Product Images from "The central region of the msp gene of Treponema denticola has sequence heterogeneity among clinical samples, obtained from patients with periodontitis"

    Article Title: The central region of the msp gene of Treponema denticola has sequence heterogeneity among clinical samples, obtained from patients with periodontitis

    Journal: BMC Infectious Diseases

    doi: 10.1186/1471-2334-10-345

    MSP amino acid sequence alignment of T. denticola strains ATCC 35405 and Group A (panel A), and ATCC 33520 and Group B (panel B) . The grey areas indicate single amino acid substitutions compared with ATCC 35405 (panel A) and ATCC 33520 (panel B).
    Figure Legend Snippet: MSP amino acid sequence alignment of T. denticola strains ATCC 35405 and Group A (panel A), and ATCC 33520 and Group B (panel B) . The grey areas indicate single amino acid substitutions compared with ATCC 35405 (panel A) and ATCC 33520 (panel B).

    Techniques Used: Sequencing

    Diversity of msp sequences . Sequence alignments of 17 central regions (from 600 to 900 nucleotides) from T. denticola positive clinical specimens. In panel A are shown the clinical samples of Group A. In panel B are shown the clinical samples of Group B. The upper line contains the sequence of T. denticola strain ATCC 35405 and ATCC 33520, respectively, in both panels. The grey areas indicate variations of single nucleotide positions compared with T. denticola ATCC 35405.
    Figure Legend Snippet: Diversity of msp sequences . Sequence alignments of 17 central regions (from 600 to 900 nucleotides) from T. denticola positive clinical specimens. In panel A are shown the clinical samples of Group A. In panel B are shown the clinical samples of Group B. The upper line contains the sequence of T. denticola strain ATCC 35405 and ATCC 33520, respectively, in both panels. The grey areas indicate variations of single nucleotide positions compared with T. denticola ATCC 35405.

    Techniques Used: Sequencing

    Evolutionary relationships of T. denticola msp gene, deduced from the sequences of 17 clinical samples, ATCC 35405, ATCC 33520, and OTK . The phylogenetic analysis was performed using the neighbor-joining method with MEGA 4 on aligned sequences from the msp complete cds sequence (bootstrap values > 75 are shown at nodes).
    Figure Legend Snippet: Evolutionary relationships of T. denticola msp gene, deduced from the sequences of 17 clinical samples, ATCC 35405, ATCC 33520, and OTK . The phylogenetic analysis was performed using the neighbor-joining method with MEGA 4 on aligned sequences from the msp complete cds sequence (bootstrap values > 75 are shown at nodes).

    Techniques Used: Sequencing

    Antigenicity plot of T. denticola strains ATCC 35405 (frame A), ATCC 33520 (frame B), and 2 representative specimens (B66, frame C; B23, frame D) . In each frame, the area of the plot that is surrounded by a continuous line represents the central region of MSP. The internal smaller area, surrounded by the dotted line, represents the portion that has the greatest difference in predicted antigenicity between specimens B66 and B23 and ATCC35405.
    Figure Legend Snippet: Antigenicity plot of T. denticola strains ATCC 35405 (frame A), ATCC 33520 (frame B), and 2 representative specimens (B66, frame C; B23, frame D) . In each frame, the area of the plot that is surrounded by a continuous line represents the central region of MSP. The internal smaller area, surrounded by the dotted line, represents the portion that has the greatest difference in predicted antigenicity between specimens B66 and B23 and ATCC35405.

    Techniques Used:

    67) Product Images from "Characterization of a potential ABC-type bacteriocin exporter protein from Treponema denticola"

    Article Title: Characterization of a potential ABC-type bacteriocin exporter protein from Treponema denticola

    Journal: BMC Oral Health

    doi: 10.1186/s12903-016-0243-7

    Southern blot analysis of tepA1 ( a ), tepA2 ( b ) , and tepA3 ( c ). Genomic DNA from T. denticola strains was digested with Hin dIII. 1: genomic DNA from ATCC 33520, 2: genomic DNA from ATCC 33521, genomic DNA from ATCC 35404, 4: genomic DNA from ATCC 35405, 5: genomic DNA from GM1
    Figure Legend Snippet: Southern blot analysis of tepA1 ( a ), tepA2 ( b ) , and tepA3 ( c ). Genomic DNA from T. denticola strains was digested with Hin dIII. 1: genomic DNA from ATCC 33520, 2: genomic DNA from ATCC 33521, genomic DNA from ATCC 35404, 4: genomic DNA from ATCC 35405, 5: genomic DNA from GM1

    Techniques Used: Southern Blot

    68) Product Images from "Binding Properties and Adhesion-Mediating Regions of the Major Sheath Protein of Treponema denticola ATCC 35405"

    Article Title: Binding Properties and Adhesion-Mediating Regions of the Major Sheath Protein of Treponema denticola ATCC 35405

    Journal: Infection and Immunity

    doi: 10.1128/IAI.73.5.2891-2898.2005

    Interactions of rMsp antibodies with T. denticola ATCC 35405 cells and of whole-cell antibodies with rMsp fragments. (Panel A) Reactivity in ELISA of antiserum (1:250 diluted) to T. denticola ATCC 35405 cells (W) or antisera (1:250 diluted) raised to
    Figure Legend Snippet: Interactions of rMsp antibodies with T. denticola ATCC 35405 cells and of whole-cell antibodies with rMsp fragments. (Panel A) Reactivity in ELISA of antiserum (1:250 diluted) to T. denticola ATCC 35405 cells (W) or antisera (1:250 diluted) raised to

    Techniques Used: Enzyme-linked Immunosorbent Assay

    Reactivities of Msp antisera with T. denticola ATCC 35405 outer membrane protein extracts. (Panel A) SDS-PAGE gel of outer membrane proteins. (Panel B) Western blots reacted with antisera to rN-Msp (lane 1), rV-Msp (lane 2), or rC-Msp (lane 3). Molecular
    Figure Legend Snippet: Reactivities of Msp antisera with T. denticola ATCC 35405 outer membrane protein extracts. (Panel A) SDS-PAGE gel of outer membrane proteins. (Panel B) Western blots reacted with antisera to rN-Msp (lane 1), rV-Msp (lane 2), or rC-Msp (lane 3). Molecular

    Techniques Used: SDS Page, Western Blot

    Binding of rMsp to human fibronectin and to 30-kDa N-terminal fragment of human fibronectin. (Panel A) Western blot overlay of trypsin-derived fragments of human plasma fibronectin reacted with rMsp (lane 1) or with biotinylated T. denticola ATCC 35405
    Figure Legend Snippet: Binding of rMsp to human fibronectin and to 30-kDa N-terminal fragment of human fibronectin. (Panel A) Western blot overlay of trypsin-derived fragments of human plasma fibronectin reacted with rMsp (lane 1) or with biotinylated T. denticola ATCC 35405

    Techniques Used: Binding Assay, Western Blot, Derivative Assay

    Diagrammatic representation of the Msp sequences from T. denticola ATCC 35520 (A), strain ATCC 35405 (B), and of recombinant Msp polypeptides rMsp (530 aa residues), rN-Msp (189 aa residues), rV-Msp (57 aa residues), and rN-Msp (272 aa residues), with
    Figure Legend Snippet: Diagrammatic representation of the Msp sequences from T. denticola ATCC 35520 (A), strain ATCC 35405 (B), and of recombinant Msp polypeptides rMsp (530 aa residues), rN-Msp (189 aa residues), rV-Msp (57 aa residues), and rN-Msp (272 aa residues), with

    Techniques Used: Recombinant

    Effect of exogenously added rMsp on adhesion of Treponema strains to immobilized human fibronectin or 30-kDa fibronectin fragment. (Panel A) Adhesion levels of T. denticola ATCC 35405 cells to 0.1 μg fibronectin (filled column) or 30-kDa fibronectin
    Figure Legend Snippet: Effect of exogenously added rMsp on adhesion of Treponema strains to immobilized human fibronectin or 30-kDa fibronectin fragment. (Panel A) Adhesion levels of T. denticola ATCC 35405 cells to 0.1 μg fibronectin (filled column) or 30-kDa fibronectin

    Techniques Used:

    69) Product Images from "Genome-Wide Relatedness of Treponema pedis, from Gingiva and Necrotic Skin Lesions of Pigs, with the Human Oral Pathogen Treponema denticola"

    Article Title: Genome-Wide Relatedness of Treponema pedis, from Gingiva and Necrotic Skin Lesions of Pigs, with the Human Oral Pathogen Treponema denticola

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0071281

    Circular representation of the T. pedis T A4 genome and complete genome alignment with T. denticola . (A.) Circular representation of the T. pedis T A4 genome. The CDSs are shown in violet where the outer circle represents predictions on the plus strand and the second circle those on the minus strand. CDSs with a best BLASTP hit in T. denticola ATCC 35405 are colored red and shown in the third circle. The fourth circle represents genes with best BLASTP hits in T. brennaborense (black), F. nucleatum (green), F. alocis (blue) and T. succinifaciens (grey). G+C skew is drawn in the inner circle. (B.) Complete genome alignment between T. pedis T A4 and T. denticola ATCC 35405. Dots represent maximum unique matches (MUMs) between the genomes. MUMs oriented in the same direction are depicted as red dots and reverse complemented MUMs are depicted as blue dots.
    Figure Legend Snippet: Circular representation of the T. pedis T A4 genome and complete genome alignment with T. denticola . (A.) Circular representation of the T. pedis T A4 genome. The CDSs are shown in violet where the outer circle represents predictions on the plus strand and the second circle those on the minus strand. CDSs with a best BLASTP hit in T. denticola ATCC 35405 are colored red and shown in the third circle. The fourth circle represents genes with best BLASTP hits in T. brennaborense (black), F. nucleatum (green), F. alocis (blue) and T. succinifaciens (grey). G+C skew is drawn in the inner circle. (B.) Complete genome alignment between T. pedis T A4 and T. denticola ATCC 35405. Dots represent maximum unique matches (MUMs) between the genomes. MUMs oriented in the same direction are depicted as red dots and reverse complemented MUMs are depicted as blue dots.

    Techniques Used:

    70) Product Images from "Motility and Chemotaxis in Tissue Penetration of Oral Epithelial Cell Layers by Treponema denticola"

    Article Title: Motility and Chemotaxis in Tissue Penetration of Oral Epithelial Cell Layers by Treponema denticola

    Journal: Infection and Immunity

    doi: 10.1128/IAI.69.10.6276-6283.2001

    Motility of wild-type T. denticola ATCC 35405 in KBM for epithelial cell lines in a 5% CO 2 atmosphere at 35°C (○) and under anaerobic conditions (85% N 2 , 10% H 2 , 5% CO 2 ) at 35°C (□). Values for each condition were obtained in triplicate in two independent experiments. More than 600 cells were examined for cellular motility in each experiment. All mutant derivatives except the nonmotile strain HL53 showed similar results (data not shown).
    Figure Legend Snippet: Motility of wild-type T. denticola ATCC 35405 in KBM for epithelial cell lines in a 5% CO 2 atmosphere at 35°C (○) and under anaerobic conditions (85% N 2 , 10% H 2 , 5% CO 2 ) at 35°C (□). Values for each condition were obtained in triplicate in two independent experiments. More than 600 cells were examined for cellular motility in each experiment. All mutant derivatives except the nonmotile strain HL53 showed similar results (data not shown).

    Techniques Used: Mutagenesis

    71) Product Images from "Identification of a Treponema denticola OppA Homologue That Binds Host Proteins Present in the Subgingival Environment"

    Article Title: Identification of a Treponema denticola OppA Homologue That Binds Host Proteins Present in the Subgingival Environment

    Journal: Infection and Immunity

    doi:

    Binding of soluble host proteins to T. denticola cells and proteins. (A) ELISA format. FN, plasminogen (Pgn), or BSA in PBS were added to wells containing immobilized T. denticola ATCC 35405 cells (T.d.), native OppA (OppA), recombinant LacZ-OppA fusion protein (rOppA40), recombinant Msp (rMsp), or BSA. Bound FN and plasminogen were detected with anti-FN (shaded bars) and anti-plasminogen (hatched bars) antibodies, respectively. The y axis shows absorbance at 405 nm. Data shown represent the means ± standard deviations of at least two experiments using triplicate samples. (B) Ligand blot format. Duplicate samples of protein (1 μg) or cells (0.1 ml, OD 600 = 0.2) applied to nitrocellulose membranes were probed with plasminogen (samples 2 to 4) or plasminogen plus EACA (sample 5). Bound plasminogen was detected with anti-plasminogen immunoglobulin G. Lanes: 1, Plasminogen; 2, 5, and 6, T. denticola ATCC 35405; 3, T. denticola OHE; 4, T. denticola MHE.
    Figure Legend Snippet: Binding of soluble host proteins to T. denticola cells and proteins. (A) ELISA format. FN, plasminogen (Pgn), or BSA in PBS were added to wells containing immobilized T. denticola ATCC 35405 cells (T.d.), native OppA (OppA), recombinant LacZ-OppA fusion protein (rOppA40), recombinant Msp (rMsp), or BSA. Bound FN and plasminogen were detected with anti-FN (shaded bars) and anti-plasminogen (hatched bars) antibodies, respectively. The y axis shows absorbance at 405 nm. Data shown represent the means ± standard deviations of at least two experiments using triplicate samples. (B) Ligand blot format. Duplicate samples of protein (1 μg) or cells (0.1 ml, OD 600 = 0.2) applied to nitrocellulose membranes were probed with plasminogen (samples 2 to 4) or plasminogen plus EACA (sample 5). Bound plasminogen was detected with anti-plasminogen immunoglobulin G. Lanes: 1, Plasminogen; 2, 5, and 6, T. denticola ATCC 35405; 3, T. denticola OHE; 4, T. denticola MHE.

    Techniques Used: Binding Assay, Enzyme-linked Immunosorbent Assay, Recombinant

    Confirmation of construction of allelic replacement mutants in the opp locus. (A) Southern blots of Sca I-digested T. denticola genomic DNA were probed with a biotinylated internal oppA fragment ( opp ) and the 2.1-kb ermF/AM cassette ( erm ). The ermF/AM cassette contains a single Sca I site. (B) Western immunoblot of T. denticola lysates probed with anti-70 antibodies. Lanes: 1, parent strain ATCC 35405; 2, oppA mutant strain OHE; 3, oppF mutant strain OXE.
    Figure Legend Snippet: Confirmation of construction of allelic replacement mutants in the opp locus. (A) Southern blots of Sca I-digested T. denticola genomic DNA were probed with a biotinylated internal oppA fragment ( opp ) and the 2.1-kb ermF/AM cassette ( erm ). The ermF/AM cassette contains a single Sca I site. (B) Western immunoblot of T. denticola lysates probed with anti-70 antibodies. Lanes: 1, parent strain ATCC 35405; 2, oppA mutant strain OHE; 3, oppF mutant strain OXE.

    Techniques Used: Western Blot, Mutagenesis

    Conservation of oppA in oral Treponema strains. (A) Southern blot of Hin dIII-digested chromosomal DNA probed with a 0.9-kb internal fragment of oppA . (B) Western blot of whole-cell extracts probed with anti-40 antibodies. Lanes: 1, T. denticola ATCC 35405; 2, T. denticola ATCC 35404; 3, T. denticola ATCC 33520; 4, T. vincentii LA-1; 5, T. denticola OTK; 6, T. denticola GM-1; 7, T. socranskii ATCC 35536; 8, T. pectinovorum ATCC 33768.
    Figure Legend Snippet: Conservation of oppA in oral Treponema strains. (A) Southern blot of Hin dIII-digested chromosomal DNA probed with a 0.9-kb internal fragment of oppA . (B) Western blot of whole-cell extracts probed with anti-40 antibodies. Lanes: 1, T. denticola ATCC 35405; 2, T. denticola ATCC 35404; 3, T. denticola ATCC 33520; 4, T. vincentii LA-1; 5, T. denticola OTK; 6, T. denticola GM-1; 7, T. socranskii ATCC 35536; 8, T. pectinovorum ATCC 33768.

    Techniques Used: Southern Blot, Western Blot

    72) Product Images from "Treponema denticola PrcB Is Required for Expression and Activity of the PrcA-PrtP (Dentilisin) Complex ▿"

    Article Title: Treponema denticola PrcB Is Required for Expression and Activity of the PrcA-PrtP (Dentilisin) Complex ▿

    Journal: Journal of Bacteriology

    doi: 10.1128/JB.00274-10

    Conservation of prcB in T. denticola . The deduced amino acid sequence of the complete ORF, including the PrcB coding region, is shown for T. denticola strains ATCC 35405, ATCC 33520, and OTK, aligned using Clustal 2.0. The N-terminal valine residue predicted by JCVI (Val 38 ) and the two possible N-terminal methionine residues (Met 1 and Met 7 ) predicted by the present study are shaded gray. The predicted signal peptidase II cleavage site is indicated by a black arrowhead. Amino acid identity throughout all three sequences is indicated by asterisks. Conserved and semiconserved amino acids are shown by colons and dots, respectively.
    Figure Legend Snippet: Conservation of prcB in T. denticola . The deduced amino acid sequence of the complete ORF, including the PrcB coding region, is shown for T. denticola strains ATCC 35405, ATCC 33520, and OTK, aligned using Clustal 2.0. The N-terminal valine residue predicted by JCVI (Val 38 ) and the two possible N-terminal methionine residues (Met 1 and Met 7 ) predicted by the present study are shaded gray. The predicted signal peptidase II cleavage site is indicated by a black arrowhead. Amino acid identity throughout all three sequences is indicated by asterisks. Conserved and semiconserved amino acids are shown by colons and dots, respectively.

    Techniques Used: Sequencing

    73) Product Images from "Filamentous Actin Disruption and Diminished Inositol Phosphate Response in Gingival Fibroblasts Caused by Treponema denticola"

    Article Title: Filamentous Actin Disruption and Diminished Inositol Phosphate Response in Gingival Fibroblasts Caused by Treponema denticola

    Journal: Infection and Immunity

    doi:

    Histogram of fluorescence intensity of rhodamine-phalloidin-labeled F-actin in HGF during a 140-min time course, analyzed by confocal microscopy. There was significant depolymerization of F-actin in the T. denticola ATCC 35405-challenged HGF (left graph) in comparison with the control HGF (right graph). The degree of diminished fluorescence in T. denticola -challenged cells was significant at 60 min ( P
    Figure Legend Snippet: Histogram of fluorescence intensity of rhodamine-phalloidin-labeled F-actin in HGF during a 140-min time course, analyzed by confocal microscopy. There was significant depolymerization of F-actin in the T. denticola ATCC 35405-challenged HGF (left graph) in comparison with the control HGF (right graph). The degree of diminished fluorescence in T. denticola -challenged cells was significant at 60 min ( P

    Techniques Used: Fluorescence, Labeling, Confocal Microscopy

    Comparison of filamentous actin disruption (mean ± standard deviation) in HGF challenged with different concentrations of whole cells of T. denticola ATCC 35405 (□) and OM extract (▪). The dry weight for the OM and the dry weight for the T. denticola cells were equivalent at each optical density (OD) point shown on the x axis.
    Figure Legend Snippet: Comparison of filamentous actin disruption (mean ± standard deviation) in HGF challenged with different concentrations of whole cells of T. denticola ATCC 35405 (□) and OM extract (▪). The dry weight for the OM and the dry weight for the T. denticola cells were equivalent at each optical density (OD) point shown on the x axis.

    Techniques Used: Standard Deviation

    Qualitative comparison by SDS-PAGE of T. denticola ATCC 35405 whole cells (lane 1), OM extract run at the same time (lane 2), and repeat of the OM extract run in a different gel to resolve mid-range bands more clearly (lane 3). The positions of molecular size standards (broad-range SDS-PAGE standards; Bio-Rad) are shown in kilodaltons at the left. Conditions were as follows: Washed T. denticola suspensions (optical density of 1.2 at 550 nm) from 3-day cultures or undiluted OM extract were mixed 1:1 with sample buffer (0.25 M Tris-HCl [pH 6.8], 20% glycerol, 4.6% SDS, 0.02% bromophenol blue, 10% β-mercaptoethanol) and boiled for 10 min; 25 μl was added to each lane of a 1-mm-thick Ready Gel (Bio-Rad) with a 4% stacking gel and 12% resolving gel. Electrophoresis was run in a Mini-Protean II cell (Bio-Rad). Whole cells and OM extract had several bands in common.
    Figure Legend Snippet: Qualitative comparison by SDS-PAGE of T. denticola ATCC 35405 whole cells (lane 1), OM extract run at the same time (lane 2), and repeat of the OM extract run in a different gel to resolve mid-range bands more clearly (lane 3). The positions of molecular size standards (broad-range SDS-PAGE standards; Bio-Rad) are shown in kilodaltons at the left. Conditions were as follows: Washed T. denticola suspensions (optical density of 1.2 at 550 nm) from 3-day cultures or undiluted OM extract were mixed 1:1 with sample buffer (0.25 M Tris-HCl [pH 6.8], 20% glycerol, 4.6% SDS, 0.02% bromophenol blue, 10% β-mercaptoethanol) and boiled for 10 min; 25 μl was added to each lane of a 1-mm-thick Ready Gel (Bio-Rad) with a 4% stacking gel and 12% resolving gel. Electrophoresis was run in a Mini-Protean II cell (Bio-Rad). Whole cells and OM extract had several bands in common.

    Techniques Used: SDS Page, Nucleic Acid Electrophoresis

    74) Product Images from "Treponema denticola TroR is a manganese- and iron-dependent transcriptional repressor"

    Article Title: Treponema denticola TroR is a manganese- and iron-dependent transcriptional repressor

    Journal: Molecular Microbiology

    doi: 10.1111/j.1365-2958.2008.06418.x

    TroR Td deletion mutants exhibit variable repressor activity in E. coli . A. Physical maps of wild type and C-terminally truncated TroR Td proteins. TroR Td proteins are represented as grey lines and amino acid deletions are indicated. Names of the strains expressing the various TroR Td deletion constructs in the presence of pTDE100 ( T. denticola tro P/O- lacZ reporter) or pPAL100 ( T. pallidum tro P/O- lacZ reporter) are also indicated. DtxR secondary structure is indicated: α-helices (α1, 2, 4, 5, 6) are shown in black, the DNA recognition helix (α3) is shown as a hatched line, β-strands (β1–2) are shown in grey, the proline-containing tether region (α7) is shown in black and SH3-like domain is shown in white. Full-length and mutant troR alleles were PCR-amplified from T. denticola ATCC 35405 chromosomal DNA and cloned into the NcoI and HindIII restriction sites of pBAD/HisA to facilitate the expression of TroR Td proteins. B. Immunoblot analysis of full-length and truncated TroR Td proteins expressed by: DEN113, DEN113A, DEN113B, DEN113C, DEN113D and DEN100. Effect of C-terminal deletion mutations on the expression of (C) pTDE100 or (D) pTPA100 reporter constructs. E. coli TOP10 cells harbouring both a TroR Td expression construct and a tro -P/O- lacZ reporter plasmid were grown aerobically overnight in LBL media. β-Galactosidase activity of the 12 h cultures was determined as described by Miller (1972) . Results represent the means and standard deviations of three independent experiments.
    Figure Legend Snippet: TroR Td deletion mutants exhibit variable repressor activity in E. coli . A. Physical maps of wild type and C-terminally truncated TroR Td proteins. TroR Td proteins are represented as grey lines and amino acid deletions are indicated. Names of the strains expressing the various TroR Td deletion constructs in the presence of pTDE100 ( T. denticola tro P/O- lacZ reporter) or pPAL100 ( T. pallidum tro P/O- lacZ reporter) are also indicated. DtxR secondary structure is indicated: α-helices (α1, 2, 4, 5, 6) are shown in black, the DNA recognition helix (α3) is shown as a hatched line, β-strands (β1–2) are shown in grey, the proline-containing tether region (α7) is shown in black and SH3-like domain is shown in white. Full-length and mutant troR alleles were PCR-amplified from T. denticola ATCC 35405 chromosomal DNA and cloned into the NcoI and HindIII restriction sites of pBAD/HisA to facilitate the expression of TroR Td proteins. B. Immunoblot analysis of full-length and truncated TroR Td proteins expressed by: DEN113, DEN113A, DEN113B, DEN113C, DEN113D and DEN100. Effect of C-terminal deletion mutations on the expression of (C) pTDE100 or (D) pTPA100 reporter constructs. E. coli TOP10 cells harbouring both a TroR Td expression construct and a tro -P/O- lacZ reporter plasmid were grown aerobically overnight in LBL media. β-Galactosidase activity of the 12 h cultures was determined as described by Miller (1972) . Results represent the means and standard deviations of three independent experiments.

    Techniques Used: Activity Assay, Expressing, Construct, Mutagenesis, Polymerase Chain Reaction, Amplification, Clone Assay, Plasmid Preparation

    75) Product Images from "Characterization of a potential ABC-type bacteriocin exporter protein from Treponema denticola"

    Article Title: Characterization of a potential ABC-type bacteriocin exporter protein from Treponema denticola

    Journal: BMC Oral Health

    doi: 10.1186/s12903-016-0243-7

    Southern blot analysis of tepA1 ( a ), tepA2 ( b ) , and tepA3 ( c ). Genomic DNA from T. denticola strains was digested with Hin dIII. 1: genomic DNA from ATCC 33520, 2: genomic DNA from ATCC 33521, genomic DNA from ATCC 35404, 4: genomic DNA from ATCC 35405, 5: genomic DNA from GM1
    Figure Legend Snippet: Southern blot analysis of tepA1 ( a ), tepA2 ( b ) , and tepA3 ( c ). Genomic DNA from T. denticola strains was digested with Hin dIII. 1: genomic DNA from ATCC 33520, 2: genomic DNA from ATCC 33521, genomic DNA from ATCC 35404, 4: genomic DNA from ATCC 35405, 5: genomic DNA from GM1

    Techniques Used: Southern Blot

    Related Articles

    Centrifugation:

    Article Title: Immunotopological Analysis of the Treponema denticola Major Surface Protein (Msp)
    Article Snippet: Protein expression was induced by the addition of isopropyl-β- d -thiogalactopyranoside (IPTG) to 0.2 mM, and the culture was further incubated for 3 h. Cells were collected by centrifugation for 10 min at 4,000 rpm and lysed by suspension in 1× Laemmli sample buffer and repeated passage through a 26-gauge needle. .. Samples were subjected to 10% SDS-PAGE and analyzed by Western blotting with rabbit antibodies raised against the ATCC 35405 Msp N-terminal domain (residues 14 to 202) , native ATCC 35405 Msp (this study), recombinant Msp , T. denticola ATCC 35405 cells , or T. denticola FlaA ( ).

    Mass Spectrometry:

    Article Title: Major Membrane Protein TDE2508 Regulates Adhesive Potency in Treponema denticola
    Article Snippet: Analysis of Major Membrane-Associated Proteins in T . denticola We analyzed the major proteins of the envelope (membrane) fraction in T . denticola ATCC 35405. .. The major proteins (i.e., intense bands containing more than 100 ng of protein or 1% of total protein) were analyzed by mass spectrometry, and 16 proteins were identified ( and ).

    Synthesized:

    Article Title: Characterization of a potential ABC-type bacteriocin exporter protein from Treponema denticola
    Article Snippet: DNA microarray analysis T. denticola ATCC 35405 and KT-3 were cultured as described above for 2 days. .. DNase treatment was carried out using a TURBO DNA-free kit Life Technologies). cDNA was synthesized using a SuperScript Double-Stranded cDNA Synthesis kit (Invitrogen).

    Blocking Assay:

    Article Title: Binding Properties and Adhesion-Mediating Regions of the Major Sheath Protein of Treponema denticola ATCC 35405
    Article Snippet: .. Receptor blocking experiments using rMsp from T. denticola ATCC 35405 confirmed that the N-terminal region of fibronectin is the only region targeted in vitro by T. denticola ATCC 35405. ..

    Microarray:

    Article Title: Characterization of a potential ABC-type bacteriocin exporter protein from Treponema denticola
    Article Snippet: .. DNA microarray analysis T. denticola ATCC 35405 and KT-3 were cultured as described above for 2 days. .. To investigate the relation between inactivation of tepA 2 and increase of chloramphenicol resistance, exponentially growing cells (OD660 ~ 0.2) were incubated with chloramphenicol (1 μg/ml) for 4 h. The cells were harvested immediately after chloramphenicol treatment and total RNA was extracted using Trizol (Life Technologies).

    Incubation:

    Article Title: Major Membrane Protein TDE2508 Regulates Adhesive Potency in Treponema denticola
    Article Snippet: The plates were anaerobically incubated at 37°C, and the turbid plaque was monitored for 2 weeks as an index of bacterial motility. .. For the autoaggregation test, T . denticola ATCC 35405 (open circle) and tde2508 -deletion mutant (open triangle) were set in a cuvette, and the optical density at 600 nm (OD600) was monitored.

    Article Title: Immunotopological Analysis of the Treponema denticola Major Surface Protein (Msp)
    Article Snippet: Protein expression was induced by the addition of isopropyl-β- d -thiogalactopyranoside (IPTG) to 0.2 mM, and the culture was further incubated for 3 h. Cells were collected by centrifugation for 10 min at 4,000 rpm and lysed by suspension in 1× Laemmli sample buffer and repeated passage through a 26-gauge needle. .. Samples were subjected to 10% SDS-PAGE and analyzed by Western blotting with rabbit antibodies raised against the ATCC 35405 Msp N-terminal domain (residues 14 to 202) , native ATCC 35405 Msp (this study), recombinant Msp , T. denticola ATCC 35405 cells , or T. denticola FlaA ( ).

    Article Title: Characterization of a potential ABC-type bacteriocin exporter protein from Treponema denticola
    Article Snippet: DNA microarray analysis T. denticola ATCC 35405 and KT-3 were cultured as described above for 2 days. .. To investigate the relation between inactivation of tepA 2 and increase of chloramphenicol resistance, exponentially growing cells (OD660 ~ 0.2) were incubated with chloramphenicol (1 μg/ml) for 4 h. The cells were harvested immediately after chloramphenicol treatment and total RNA was extracted using Trizol (Life Technologies).

    Activity Assay:

    Article Title: Genome-Wide Relatedness of Treponema pedis, from Gingiva and Necrotic Skin Lesions of Pigs, with the Human Oral Pathogen Treponema denticola
    Article Snippet: These include the dentilisin operon in T. denticola , which is believed to contribute to periodontal disease by interfering with host signaling pathways and degrade host-cell matrix proteins by its proteolytic activity , . .. In T. denticola ATCC 35405, this operon consists of the components named PrcB, PrcA and PrtP .

    Article Title: Binding Properties and Adhesion-Mediating Regions of the Major Sheath Protein of Treponema denticola ATCC 35405
    Article Snippet: Strains of Treponema species that are deficient in CTLP activity generally show lower levels of binding to fibronectin , even though they appear to express Msp-like proteins. .. The Msp proteins from T. denticola ATCC 35405 and ATCC 35520 show high sequence identity (except for the central V region; Fig. ), whereas the Msp polypeptide from T. denticola OTK is significantly different and antigenically distinct ( ).

    Expressing:

    Article Title: Binding Properties and Adhesion-Mediating Regions of the Major Sheath Protein of Treponema denticola ATCC 35405
    Article Snippet: In this study, recombinant Msp and defined fragments were successfully purified from E. coli , with no deleterious effects on the expression host and with minimal degradation of recombinant polypeptides. .. Receptor blocking experiments using rMsp from T. denticola ATCC 35405 confirmed that the N-terminal region of fibronectin is the only region targeted in vitro by T. denticola ATCC 35405.

    Article Title: Immunotopological Analysis of the Treponema denticola Major Surface Protein (Msp)
    Article Snippet: Paragraph title: Expression of recombinant proteins in E. coli . ... Samples were subjected to 10% SDS-PAGE and analyzed by Western blotting with rabbit antibodies raised against the ATCC 35405 Msp N-terminal domain (residues 14 to 202) , native ATCC 35405 Msp (this study), recombinant Msp , T. denticola ATCC 35405 cells , or T. denticola FlaA ( ).

    Article Title: Characterization of a potential ABC-type bacteriocin exporter protein from Treponema denticola
    Article Snippet: DNA microarray analysis T. denticola ATCC 35405 and KT-3 were cultured as described above for 2 days. .. DNA microarray gene expression analysis was carried out using Roche NimbleGen custom arrays (2006-07-27_TI243275_60mer; Roche, Indianapolis, IN) according to the standard NimbleGen procedure (NimbleGen arrays user’s guide: gene expression analysis, v6.0).

    Western Blot:

    Article Title: Immunotopological Analysis of the Treponema denticola Major Surface Protein (Msp)
    Article Snippet: .. Samples were subjected to 10% SDS-PAGE and analyzed by Western blotting with rabbit antibodies raised against the ATCC 35405 Msp N-terminal domain (residues 14 to 202) , native ATCC 35405 Msp (this study), recombinant Msp , T. denticola ATCC 35405 cells , or T. denticola FlaA ( ). .. SDS-PAGE and Western immunoblotting were performed as described previously ( ).

    Cell Culture:

    Article Title: Characterization of a potential ABC-type bacteriocin exporter protein from Treponema denticola
    Article Snippet: .. DNA microarray analysis T. denticola ATCC 35405 and KT-3 were cultured as described above for 2 days. .. To investigate the relation between inactivation of tepA 2 and increase of chloramphenicol resistance, exponentially growing cells (OD660 ~ 0.2) were incubated with chloramphenicol (1 μg/ml) for 4 h. The cells were harvested immediately after chloramphenicol treatment and total RNA was extracted using Trizol (Life Technologies).

    Sequencing:

    Article Title: Binding Properties and Adhesion-Mediating Regions of the Major Sheath Protein of Treponema denticola ATCC 35405
    Article Snippet: .. The msp gene of T. denticola ATCC 35405 may be divided into three coding regions on the basis of sequence conservation with msp of T. denticola ATCC 33520 (Fig. ). .. These comprise an N-terminal region of 609 bp; a central, sequence variable (V) region of approximately 200 bp; and a C-terminal region of about 800 bp (Fig. ).

    Article Title: Binding Properties and Adhesion-Mediating Regions of the Major Sheath Protein of Treponema denticola ATCC 35405
    Article Snippet: .. The Msp proteins from T. denticola ATCC 35405 and ATCC 35520 show high sequence identity (except for the central V region; Fig. ), whereas the Msp polypeptide from T. denticola OTK is significantly different and antigenically distinct ( ). .. The predicted sequence of Msp from T. denticola GM-1 is > 95% identical to that of Msp from strain OTK (A. M. Edwards, unpublished data).

    Article Title: Genome-Wide Relatedness of Treponema pedis, from Gingiva and Necrotic Skin Lesions of Pigs, with the Human Oral Pathogen Treponema denticola
    Article Snippet: Annotation of T. pedis T A4 Coding DNA sequence (CDS) positions in T. pedis T A4 were predicted with Glimmer 3 . .. Positions of the ribosomal subunit (rRNA) genes 16S, 23S and 5S were identified by pair-wise nucleotide comparisons with corresponding genes in T. denticola ATCC 35405.

    Article Title: Genome-Wide Relatedness of Treponema pedis, from Gingiva and Necrotic Skin Lesions of Pigs, with the Human Oral Pathogen Treponema denticola
    Article Snippet: To gain insight into the genetic composition of T. pedis and to identify potential virulence factors, we determined the complete genome sequence of the T. pedis strain T A4, isolated from a case of pig ear necrosis. .. The wide set of T. pedis genes was compared to genes in T. denticola ATCC 35405 complemented with genes from 12 additional T. denticola draft WGS assemblies.

    Binding Assay:

    Article Title: Binding Properties and Adhesion-Mediating Regions of the Major Sheath Protein of Treponema denticola ATCC 35405
    Article Snippet: These fibronectin interaction properties of Msp are similar to those of T. denticola cells and to those of T. vincentii and related Treponema species ( ). rMsp was found to block, by up to 50%, binding of T. denticola ATCC 35405 cells to fibronectin, an observation that conflicts with a previous report showing that full-length recombinant Msp did not significantly affect adhesion to fibronectin ( ). .. Receptor blocking experiments using rMsp from T. denticola ATCC 35405 confirmed that the N-terminal region of fibronectin is the only region targeted in vitro by T. denticola ATCC 35405.

    Article Title: Binding Properties and Adhesion-Mediating Regions of the Major Sheath Protein of Treponema denticola ATCC 35405
    Article Snippet: Paragraph title: Binding regions of Msp to fibronectin and other host proteins. ... The msp gene of T. denticola ATCC 35405 may be divided into three coding regions on the basis of sequence conservation with msp of T. denticola ATCC 33520 (Fig. ).

    Article Title: Binding Properties and Adhesion-Mediating Regions of the Major Sheath Protein of Treponema denticola ATCC 35405
    Article Snippet: Strains of T. socranskii and T. pectinovorum have been shown to produce 43-kDa Msp-like proteins , but their binding properties and their relationship to other Msp proteins from T. denticola are unknown. .. The Msp proteins from T. denticola ATCC 35405 and ATCC 35520 show high sequence identity (except for the central V region; Fig. ), whereas the Msp polypeptide from T. denticola OTK is significantly different and antigenically distinct ( ).

    In Vivo:

    Article Title: Binding Properties and Adhesion-Mediating Regions of the Major Sheath Protein of Treponema denticola ATCC 35405
    Article Snippet: Thus, it is likely that CTLP ( ) or other components of the Msp complex may modulate fibronectin binding functions in vivo. .. The Msp proteins from T. denticola ATCC 35405 and ATCC 35520 show high sequence identity (except for the central V region; Fig. ), whereas the Msp polypeptide from T. denticola OTK is significantly different and antigenically distinct ( ).

    Mutagenesis:

    Article Title: Major Membrane Protein TDE2508 Regulates Adhesive Potency in Treponema denticola
    Article Snippet: .. For the autoaggregation test, T . denticola ATCC 35405 (open circle) and tde2508 -deletion mutant (open triangle) were set in a cuvette, and the optical density at 600 nm (OD600) was monitored. .. For the coaggregation test, T . denticola ATCC 35405 (closed circle) and tde2508 -deletion mutant (closed triangle) were mixed with P . gingivalis , and the OD600 was monitored.

    Article Title: Motility and Chemotaxis in Tissue Penetration of Oral Epithelial Cell Layers by Treponema denticola
    Article Snippet: .. Wild-type T. denticola ATCC 35405 was found to penetrate the tissue layers effectively, whereas a nonmotile mutant was unable to overcome the tissue barrier. .. Interestingly, the chemotaxis mutants also showed impaired tissue penetration.

    Isolation:

    Article Title: Binding Properties and Adhesion-Mediating Regions of the Major Sheath Protein of Treponema denticola ATCC 35405
    Article Snippet: The Msp proteins from T. denticola ATCC 35405 and ATCC 35520 show high sequence identity (except for the central V region; Fig. ), whereas the Msp polypeptide from T. denticola OTK is significantly different and antigenically distinct ( ). .. In contrast, T. vincentii and some related Treponema species isolated from animal infections show lower levels of binding to fibronectin than T. denticola ( ).

    Article Title: Genome-Wide Relatedness of Treponema pedis, from Gingiva and Necrotic Skin Lesions of Pigs, with the Human Oral Pathogen Treponema denticola
    Article Snippet: To gain insight into the genetic composition of T. pedis and to identify potential virulence factors, we determined the complete genome sequence of the T. pedis strain T A4, isolated from a case of pig ear necrosis. .. The wide set of T. pedis genes was compared to genes in T. denticola ATCC 35405 complemented with genes from 12 additional T. denticola draft WGS assemblies.

    Purification:

    Article Title: Binding Properties and Adhesion-Mediating Regions of the Major Sheath Protein of Treponema denticola ATCC 35405
    Article Snippet: In this study, recombinant Msp and defined fragments were successfully purified from E. coli , with no deleterious effects on the expression host and with minimal degradation of recombinant polypeptides. .. Receptor blocking experiments using rMsp from T. denticola ATCC 35405 confirmed that the N-terminal region of fibronectin is the only region targeted in vitro by T. denticola ATCC 35405.

    Article Title: Binding Properties and Adhesion-Mediating Regions of the Major Sheath Protein of Treponema denticola ATCC 35405
    Article Snippet: The msp gene of T. denticola ATCC 35405 may be divided into three coding regions on the basis of sequence conservation with msp of T. denticola ATCC 33520 (Fig. ). .. To determine if these regions encoded Msp fragments with substrate binding properties, recombinant polypeptides corresponding to sequences within the N-terminal (rN-Msp, 14 to 202 aa residues), variable (rV-Msp, 203 to 259 aa residues), and C-terminal (rC-Msp, 272 to 543 aa residues) regions were purified.

    Construct:

    Article Title: Immunotopological Analysis of the Treponema denticola Major Surface Protein (Msp)
    Article Snippet: Plasmid DNAs carrying various msp constructs were introduced into the E. coli expression strain C41/pLysS. .. Samples were subjected to 10% SDS-PAGE and analyzed by Western blotting with rabbit antibodies raised against the ATCC 35405 Msp N-terminal domain (residues 14 to 202) , native ATCC 35405 Msp (this study), recombinant Msp , T. denticola ATCC 35405 cells , or T. denticola FlaA ( ).

    SDS Page:

    Article Title: Major Membrane Protein TDE2508 Regulates Adhesive Potency in Treponema denticola
    Article Snippet: Analysis of Major Membrane-Associated Proteins in T . denticola We analyzed the major proteins of the envelope (membrane) fraction in T . denticola ATCC 35405. .. Ten micrograms of the fraction was subjected to SDS-PAGE, then stained with CBB.

    Article Title: Binding Properties and Adhesion-Mediating Regions of the Major Sheath Protein of Treponema denticola ATCC 35405
    Article Snippet: The msp gene of T. denticola ATCC 35405 may be divided into three coding regions on the basis of sequence conservation with msp of T. denticola ATCC 33520 (Fig. ). .. We were unable to express a stable recombinant polypeptide comprising the entire V region (203 to 271 aa residues). rMsp and rC-Msp migrated on SDS-PAGE according to their predicted molecular masses of 53 kDa and 31.7 kDa, respectively (Fig. , lanes 1 and 4).

    Article Title: Immunotopological Analysis of the Treponema denticola Major Surface Protein (Msp)
    Article Snippet: .. Samples were subjected to 10% SDS-PAGE and analyzed by Western blotting with rabbit antibodies raised against the ATCC 35405 Msp N-terminal domain (residues 14 to 202) , native ATCC 35405 Msp (this study), recombinant Msp , T. denticola ATCC 35405 cells , or T. denticola FlaA ( ). .. SDS-PAGE and Western immunoblotting were performed as described previously ( ).

    Plasmid Preparation:

    Article Title: Immunotopological Analysis of the Treponema denticola Major Surface Protein (Msp)
    Article Snippet: Plasmid DNAs carrying various msp constructs were introduced into the E. coli expression strain C41/pLysS. .. Samples were subjected to 10% SDS-PAGE and analyzed by Western blotting with rabbit antibodies raised against the ATCC 35405 Msp N-terminal domain (residues 14 to 202) , native ATCC 35405 Msp (this study), recombinant Msp , T. denticola ATCC 35405 cells , or T. denticola FlaA ( ).

    Functional Assay:

    Article Title: Genome-Wide Relatedness of Treponema pedis, from Gingiva and Necrotic Skin Lesions of Pigs, with the Human Oral Pathogen Treponema denticola
    Article Snippet: .. A distribution of different functional categories for the CDSs in T. pedis T A4 and T. denticola ATCC 35405 were made by performing a BLASTP search in the COG-database (clusters of orthologous groups) . ..

    Recombinant:

    Article Title: Binding Properties and Adhesion-Mediating Regions of the Major Sheath Protein of Treponema denticola ATCC 35405
    Article Snippet: These fibronectin interaction properties of Msp are similar to those of T. denticola cells and to those of T. vincentii and related Treponema species ( ). rMsp was found to block, by up to 50%, binding of T. denticola ATCC 35405 cells to fibronectin, an observation that conflicts with a previous report showing that full-length recombinant Msp did not significantly affect adhesion to fibronectin ( ). .. Receptor blocking experiments using rMsp from T. denticola ATCC 35405 confirmed that the N-terminal region of fibronectin is the only region targeted in vitro by T. denticola ATCC 35405.

    Article Title: Binding Properties and Adhesion-Mediating Regions of the Major Sheath Protein of Treponema denticola ATCC 35405
    Article Snippet: The msp gene of T. denticola ATCC 35405 may be divided into three coding regions on the basis of sequence conservation with msp of T. denticola ATCC 33520 (Fig. ). .. To determine if these regions encoded Msp fragments with substrate binding properties, recombinant polypeptides corresponding to sequences within the N-terminal (rN-Msp, 14 to 202 aa residues), variable (rV-Msp, 203 to 259 aa residues), and C-terminal (rC-Msp, 272 to 543 aa residues) regions were purified.

    Article Title: Immunotopological Analysis of the Treponema denticola Major Surface Protein (Msp)
    Article Snippet: .. Samples were subjected to 10% SDS-PAGE and analyzed by Western blotting with rabbit antibodies raised against the ATCC 35405 Msp N-terminal domain (residues 14 to 202) , native ATCC 35405 Msp (this study), recombinant Msp , T. denticola ATCC 35405 cells , or T. denticola FlaA ( ). .. SDS-PAGE and Western immunoblotting were performed as described previously ( ).

    In Vitro:

    Article Title: Binding Properties and Adhesion-Mediating Regions of the Major Sheath Protein of Treponema denticola ATCC 35405
    Article Snippet: .. Receptor blocking experiments using rMsp from T. denticola ATCC 35405 confirmed that the N-terminal region of fibronectin is the only region targeted in vitro by T. denticola ATCC 35405. ..

    Chemotaxis Assay:

    Article Title: Motility and Chemotaxis in Tissue Penetration of Oral Epithelial Cell Layers by Treponema denticola
    Article Snippet: In this study, we addressed the role of motility and chemotaxis in tissue penetration by the periodontal disease-associated oral spirochete Treponema denticola using an oral epithelial cell line-based experimental approach. .. Wild-type T. denticola ATCC 35405 was found to penetrate the tissue layers effectively, whereas a nonmotile mutant was unable to overcome the tissue barrier.

    Staining:

    Article Title: Major Membrane Protein TDE2508 Regulates Adhesive Potency in Treponema denticola
    Article Snippet: Analysis of Major Membrane-Associated Proteins in T . denticola We analyzed the major proteins of the envelope (membrane) fraction in T . denticola ATCC 35405. .. Ten micrograms of the fraction was subjected to SDS-PAGE, then stained with CBB.

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    ATCC wild type t denticola atcc 35405
    Motility of wild-type T. <t>denticola</t> <t>ATCC</t> 35405 in KBM for epithelial cell lines in a 5% CO 2 atmosphere at 35°C (○) and under anaerobic conditions (85% N 2 , 10% H 2 , 5% CO 2 ) at 35°C (□). Values for each condition were obtained in triplicate in two independent experiments. More than 600 cells were examined for cellular motility in each experiment. All mutant derivatives except the nonmotile strain HL53 showed similar results (data not shown).
    Wild Type T Denticola Atcc 35405, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Motility of wild-type T. denticola ATCC 35405 in KBM for epithelial cell lines in a 5% CO 2 atmosphere at 35°C (○) and under anaerobic conditions (85% N 2 , 10% H 2 , 5% CO 2 ) at 35°C (□). Values for each condition were obtained in triplicate in two independent experiments. More than 600 cells were examined for cellular motility in each experiment. All mutant derivatives except the nonmotile strain HL53 showed similar results (data not shown).

    Journal: Infection and Immunity

    Article Title: Motility and Chemotaxis in Tissue Penetration of Oral Epithelial Cell Layers by Treponema denticola

    doi: 10.1128/IAI.69.10.6276-6283.2001

    Figure Lengend Snippet: Motility of wild-type T. denticola ATCC 35405 in KBM for epithelial cell lines in a 5% CO 2 atmosphere at 35°C (○) and under anaerobic conditions (85% N 2 , 10% H 2 , 5% CO 2 ) at 35°C (□). Values for each condition were obtained in triplicate in two independent experiments. More than 600 cells were examined for cellular motility in each experiment. All mutant derivatives except the nonmotile strain HL53 showed similar results (data not shown).

    Article Snippet: Wild-type T. denticola ATCC 35405 was found to penetrate the tissue layers effectively, whereas a nonmotile mutant was unable to overcome the tissue barrier.

    Techniques: Mutagenesis

    Correlation of penetration rate and tissue resistance. Penetration rates were determined after 8 h of coincubation of the tissues with wild-type T. denticola . Tissue resistance was measured before and after the experiment.

    Journal: Infection and Immunity

    Article Title: Motility and Chemotaxis in Tissue Penetration of Oral Epithelial Cell Layers by Treponema denticola

    doi: 10.1128/IAI.69.10.6276-6283.2001

    Figure Lengend Snippet: Correlation of penetration rate and tissue resistance. Penetration rates were determined after 8 h of coincubation of the tissues with wild-type T. denticola . Tissue resistance was measured before and after the experiment.

    Article Snippet: Wild-type T. denticola ATCC 35405 was found to penetrate the tissue layers effectively, whereas a nonmotile mutant was unable to overcome the tissue barrier.

    Techniques:

    Tissue penetration rates (A) and motility (B) of wild-type T. denticola (Td), T. pallidum (Tp), and T. phagedenis (Tph) and various T. denticola motility and chemotaxis mutant strains. Values were determined after 8 h of coincubation of the bacteria with the tissue. Tissues used for these experiments exhibited resistances between 11 and 14Ω. More than 600 cells of each strain were examined for cellular motility.

    Journal: Infection and Immunity

    Article Title: Motility and Chemotaxis in Tissue Penetration of Oral Epithelial Cell Layers by Treponema denticola

    doi: 10.1128/IAI.69.10.6276-6283.2001

    Figure Lengend Snippet: Tissue penetration rates (A) and motility (B) of wild-type T. denticola (Td), T. pallidum (Tp), and T. phagedenis (Tph) and various T. denticola motility and chemotaxis mutant strains. Values were determined after 8 h of coincubation of the bacteria with the tissue. Tissues used for these experiments exhibited resistances between 11 and 14Ω. More than 600 cells of each strain were examined for cellular motility.

    Article Snippet: Wild-type T. denticola ATCC 35405 was found to penetrate the tissue layers effectively, whereas a nonmotile mutant was unable to overcome the tissue barrier.

    Techniques: Chemotaxis Assay, Mutagenesis

    Interactions of rMsp antibodies with T. denticola ATCC 35405 cells and of whole-cell antibodies with rMsp fragments. (Panel A) Reactivity in ELISA of antiserum (1:250 diluted) to T. denticola ATCC 35405 cells (W) or antisera (1:250 diluted) raised to

    Journal: Infection and Immunity

    Article Title: Binding Properties and Adhesion-Mediating Regions of the Major Sheath Protein of Treponema denticola ATCC 35405

    doi: 10.1128/IAI.73.5.2891-2898.2005

    Figure Lengend Snippet: Interactions of rMsp antibodies with T. denticola ATCC 35405 cells and of whole-cell antibodies with rMsp fragments. (Panel A) Reactivity in ELISA of antiserum (1:250 diluted) to T. denticola ATCC 35405 cells (W) or antisera (1:250 diluted) raised to

    Article Snippet: The msp gene of T. denticola ATCC 35405 may be divided into three coding regions on the basis of sequence conservation with msp of T. denticola ATCC 33520 (Fig. ).

    Techniques: Enzyme-linked Immunosorbent Assay

    Reactivities of Msp antisera with T. denticola ATCC 35405 outer membrane protein extracts. (Panel A) SDS-PAGE gel of outer membrane proteins. (Panel B) Western blots reacted with antisera to rN-Msp (lane 1), rV-Msp (lane 2), or rC-Msp (lane 3). Molecular

    Journal: Infection and Immunity

    Article Title: Binding Properties and Adhesion-Mediating Regions of the Major Sheath Protein of Treponema denticola ATCC 35405

    doi: 10.1128/IAI.73.5.2891-2898.2005

    Figure Lengend Snippet: Reactivities of Msp antisera with T. denticola ATCC 35405 outer membrane protein extracts. (Panel A) SDS-PAGE gel of outer membrane proteins. (Panel B) Western blots reacted with antisera to rN-Msp (lane 1), rV-Msp (lane 2), or rC-Msp (lane 3). Molecular

    Article Snippet: The msp gene of T. denticola ATCC 35405 may be divided into three coding regions on the basis of sequence conservation with msp of T. denticola ATCC 33520 (Fig. ).

    Techniques: SDS Page, Western Blot

    Binding of rMsp to human fibronectin and to 30-kDa N-terminal fragment of human fibronectin. (Panel A) Western blot overlay of trypsin-derived fragments of human plasma fibronectin reacted with rMsp (lane 1) or with biotinylated T. denticola ATCC 35405

    Journal: Infection and Immunity

    Article Title: Binding Properties and Adhesion-Mediating Regions of the Major Sheath Protein of Treponema denticola ATCC 35405

    doi: 10.1128/IAI.73.5.2891-2898.2005

    Figure Lengend Snippet: Binding of rMsp to human fibronectin and to 30-kDa N-terminal fragment of human fibronectin. (Panel A) Western blot overlay of trypsin-derived fragments of human plasma fibronectin reacted with rMsp (lane 1) or with biotinylated T. denticola ATCC 35405

    Article Snippet: The msp gene of T. denticola ATCC 35405 may be divided into three coding regions on the basis of sequence conservation with msp of T. denticola ATCC 33520 (Fig. ).

    Techniques: Binding Assay, Western Blot, Derivative Assay

    Diagrammatic representation of the Msp sequences from T. denticola ATCC 35520 (A), strain ATCC 35405 (B), and of recombinant Msp polypeptides rMsp (530 aa residues), rN-Msp (189 aa residues), rV-Msp (57 aa residues), and rN-Msp (272 aa residues), with

    Journal: Infection and Immunity

    Article Title: Binding Properties and Adhesion-Mediating Regions of the Major Sheath Protein of Treponema denticola ATCC 35405

    doi: 10.1128/IAI.73.5.2891-2898.2005

    Figure Lengend Snippet: Diagrammatic representation of the Msp sequences from T. denticola ATCC 35520 (A), strain ATCC 35405 (B), and of recombinant Msp polypeptides rMsp (530 aa residues), rN-Msp (189 aa residues), rV-Msp (57 aa residues), and rN-Msp (272 aa residues), with

    Article Snippet: The msp gene of T. denticola ATCC 35405 may be divided into three coding regions on the basis of sequence conservation with msp of T. denticola ATCC 33520 (Fig. ).

    Techniques: Recombinant

    Effect of exogenously added rMsp on adhesion of Treponema strains to immobilized human fibronectin or 30-kDa fibronectin fragment. (Panel A) Adhesion levels of T. denticola ATCC 35405 cells to 0.1 μg fibronectin (filled column) or 30-kDa fibronectin

    Journal: Infection and Immunity

    Article Title: Binding Properties and Adhesion-Mediating Regions of the Major Sheath Protein of Treponema denticola ATCC 35405

    doi: 10.1128/IAI.73.5.2891-2898.2005

    Figure Lengend Snippet: Effect of exogenously added rMsp on adhesion of Treponema strains to immobilized human fibronectin or 30-kDa fibronectin fragment. (Panel A) Adhesion levels of T. denticola ATCC 35405 cells to 0.1 μg fibronectin (filled column) or 30-kDa fibronectin

    Article Snippet: The msp gene of T. denticola ATCC 35405 may be divided into three coding regions on the basis of sequence conservation with msp of T. denticola ATCC 33520 (Fig. ).

    Techniques: