t denticola atcc 35405 cells  (ATCC)


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  • 99
    Name:
    Treponema denticola a CIP 103919 DSM 14222
    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 cells
    Binding of soluble host proteins to T. <t>denticola</t> cells and proteins. (A) ELISA format. FN, plasminogen (Pgn), or BSA in PBS were added to wells containing immobilized T. denticola <t>ATCC</t> 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.

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    Images

    1) 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

    2) 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

    3) 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

    4) 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:

    5) 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

    6) 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:

    7) 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:

    8) 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

    9) 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

    10) 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:

    11) 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

    12) 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:

    13) 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:

    Related Articles

    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) . ..

    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. ..

    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. ..

    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).

    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 ( ).

    Recombinant:

    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 ( ).

    SDS Page:

    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 ( ).

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    ATCC antiserum against t denticola atcc 35405 whole cells
    Mean areas of lesions at infection sites after challenge with T. <t>denticola</t> <t>ATCC</t> 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.
    Antiserum Against T Denticola Atcc 35405 Whole Cells, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    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.

    Journal: Journal of Bacteriology

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

    doi:

    Figure Lengend 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.

    Article Snippet: We analyzed the antigenic proteins with antiserum against T. denticola ATCC 35405 whole cells (Fig. ).

    Techniques: 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.

    Journal: Journal of Bacteriology

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

    doi:

    Figure Lengend 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.

    Article Snippet: We analyzed the antigenic proteins with antiserum against T. denticola ATCC 35405 whole cells (Fig. ).

    Techniques:

    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.

    Journal: Journal of Bacteriology

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

    doi:

    Figure Lengend 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.

    Article Snippet: We analyzed the antigenic proteins with antiserum against T. denticola ATCC 35405 whole cells (Fig. ).

    Techniques: Southern Blot, Mutagenesis, Labeling

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

    Journal: Journal of Bacteriology

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

    doi:

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

    Article Snippet: We analyzed the antigenic proteins with antiserum against T. denticola ATCC 35405 whole cells (Fig. ).

    Techniques: 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.

    Journal: Journal of Bacteriology

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

    doi:

    Figure Lengend 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.

    Article Snippet: We analyzed the antigenic proteins with antiserum against T. denticola ATCC 35405 whole cells (Fig. ).

    Techniques: SDS Page, Electrophoresis, Staining

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

    Journal: Journal of Bacteriology

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

    doi:

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

    Article Snippet: We analyzed the antigenic proteins with antiserum against T. denticola ATCC 35405 whole cells (Fig. ).

    Techniques:

    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.

    Journal: PLoS ONE

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

    doi: 10.1371/journal.pone.0071281

    Figure Lengend 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.

    Article Snippet: There were homologues in T. pedis T A4 to a T. denticola ATCC 35405 surface antigen (TDE2258) involved in co-aggregration with the oral species T. forsythia and motility genes indirectly involved in biofilm formation with other bacteria (filament protein, flagellar hook protein) were highly conserved.

    Techniques:

    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

    Journal: BMC Oral Health

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

    doi: 10.1186/s12903-016-0243-7

    Figure Lengend 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

    Article Snippet: DNA microarray analysis T. denticola ATCC 35405 and KT-3 were cultured as described above for 2 days.

    Techniques: Southern Blot

    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

    Journal: Infection and Immunity

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

    doi:

    Figure Lengend 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

    Article Snippet: The mean fluorescence per cell was significantly less for T. denticola ATCC 35405-challenged HGF than for control HGF by 60 min and all subsequent time periods ([2.15 ± 0.24] × 106 [mean ± standard error of mean] for T. denticola and [3.32 ± 0.34] × 106 for control at 60 min; P < 0.01 [Fig. ]).

    Techniques: 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.

    Journal: Infection and Immunity

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

    doi:

    Figure Lengend 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.

    Article Snippet: The mean fluorescence per cell was significantly less for T. denticola ATCC 35405-challenged HGF than for control HGF by 60 min and all subsequent time periods ([2.15 ± 0.24] × 106 [mean ± standard error of mean] for T. denticola and [3.32 ± 0.34] × 106 for control at 60 min; P < 0.01 [Fig. ]).

    Techniques: 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.

    Journal: Infection and Immunity

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

    doi:

    Figure Lengend 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.

    Article Snippet: The mean fluorescence per cell was significantly less for T. denticola ATCC 35405-challenged HGF than for control HGF by 60 min and all subsequent time periods ([2.15 ± 0.24] × 106 [mean ± standard error of mean] for T. denticola and [3.32 ± 0.34] × 106 for control at 60 min; P < 0.01 [Fig. ]).

    Techniques: SDS Page, Nucleic Acid Electrophoresis