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    ATCC t denticola strains atcc 35405
    Southern blot analysis of tepA1 ( a ), tepA2 ( b ) , and tepA3 ( c ). Genomic DNA from T. <t>denticola</t> 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
    T Denticola Strains Atcc 35405, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 57 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    ATCC t denticola strain atcc 35404
    CGase amino acid sequences from T. <t>denticola</t> strains <t>ATCC</t> 35404 and 35405. The top line in each row shows the predicted amino acid sequence for CGase from strain ATCC 35404 (this paper). The second line ). The asterisks represent amino acids that are identical in the two strains. Triangles ).
    T Denticola Strain Atcc 35404, supplied by ATCC, used in various techniques. Bioz Stars score: 94/100, based on 15 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    ATCC t denticola strains
    Northern blot analyses of the hbpA and hbpB mRNAs. (A) Total RNA was isolated from T. <t>denticola</t> ATCC 35404 grown in GM-1 medium plus 200 μM BPD or in GM-1 medium. The indicated amounts of RNA were separated on a 1% agarose gel and stained with ethidium bromide. (B and C) The RNA was then transferred to a membrane and hybridized with an hbpA probe (a 333-bp Hin dIII fragment internal to the hbpA gene) (B) or an hbpB probe (a PCR product internal to the hbpB gene) (C). Each sample in panel C contained 3 μg of total RNA.
    T Denticola Strains, supplied by ATCC, used in various techniques. Bioz Stars score: 88/100, based on 69 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    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: Msps are 53–63 kDa and the identity of the amino acid sequences between T. denticola strains ATCC 35405 and OKT is 43 % [ ].

    Techniques: Southern Blot

    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.

    Journal: Infection and Immunity

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

    doi:

    Figure Lengend 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.

    Article Snippet: The objective of the present study was to quantify and compare the adherence activity and cytotoxic effects of two important outer membrane proteins of the T. denticola type strain ATCC 35405: the pore-forming adhesin Msp, and the chymotrypsinlike protease CTLP.

    Techniques: Transmission Assay, Sonication

    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

    Journal: Infection and Immunity

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

    doi: 10.1128/IAI.05701-11

    Figure Lengend 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

    Article Snippet: T. denticola ATCC 35405 ( ) and isogenic msp mutant strain MHE ( ) were grown in NOS broth medium as previously described ( , ), with erythromycin (Em) (40 μg ml−1 ) added as appropriate.

    Techniques: Immunofluorescence

    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: Wild-type T. denticola ATCC 35405 exhibited SAAPNA-hydrolyzing activity (1.0 × 10−4 ± 0.020 × 10−4 U/1.1 × 109 cells) whereas K1 displayed little SAAPNA-hydrolyzing activity (0.010 × 10−4 ± 0.012 × 10−4 U/1.1 × 109 cells) in whole cells.

    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: Wild-type T. denticola ATCC 35405 exhibited SAAPNA-hydrolyzing activity (1.0 × 10−4 ± 0.020 × 10−4 U/1.1 × 109 cells) whereas K1 displayed little SAAPNA-hydrolyzing activity (0.010 × 10−4 ± 0.012 × 10−4 U/1.1 × 109 cells) in whole cells.

    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: Wild-type T. denticola ATCC 35405 exhibited SAAPNA-hydrolyzing activity (1.0 × 10−4 ± 0.020 × 10−4 U/1.1 × 109 cells) whereas K1 displayed little SAAPNA-hydrolyzing activity (0.010 × 10−4 ± 0.012 × 10−4 U/1.1 × 109 cells) in whole cells.

    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: Wild-type T. denticola ATCC 35405 exhibited SAAPNA-hydrolyzing activity (1.0 × 10−4 ± 0.020 × 10−4 U/1.1 × 109 cells) whereas K1 displayed little SAAPNA-hydrolyzing activity (0.010 × 10−4 ± 0.012 × 10−4 U/1.1 × 109 cells) in whole cells.

    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: Wild-type T. denticola ATCC 35405 exhibited SAAPNA-hydrolyzing activity (1.0 × 10−4 ± 0.020 × 10−4 U/1.1 × 109 cells) whereas K1 displayed little SAAPNA-hydrolyzing activity (0.010 × 10−4 ± 0.012 × 10−4 U/1.1 × 109 cells) in whole cells.

    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: Wild-type T. denticola ATCC 35405 exhibited SAAPNA-hydrolyzing activity (1.0 × 10−4 ± 0.020 × 10−4 U/1.1 × 109 cells) whereas K1 displayed little SAAPNA-hydrolyzing activity (0.010 × 10−4 ± 0.012 × 10−4 U/1.1 × 109 cells) in whole cells.

    Techniques:

    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

    Journal: Microbiology

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

    doi: 10.1099/mic.0.055939-0

    Figure Lengend 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

    Article Snippet: Zymographic analyses revealed that the approximately 95 kDa protein band in T. denticola ATCC 35405 extracts, corresponding to the CTLP complex , had strong gelatinolytic activity ( ).

    Techniques: 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

    Journal: Microbiology

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

    doi: 10.1099/mic.0.055939-0

    Figure Lengend 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

    Article Snippet: Zymographic analyses revealed that the approximately 95 kDa protein band in T. denticola ATCC 35405 extracts, corresponding to the CTLP complex , had strong gelatinolytic activity ( ).

    Techniques:

    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

    Journal: Microbiology

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

    doi: 10.1099/mic.0.055939-0

    Figure Lengend 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

    Article Snippet: Zymographic analyses revealed that the approximately 95 kDa protein band in T. denticola ATCC 35405 extracts, corresponding to the CTLP complex , had strong gelatinolytic activity ( ).

    Techniques: Fluorescence, Microscopy

    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: The T. denticola ATCC 35405 genes marked as “pseudo” were also included.

    Techniques:

    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.

    Journal: Infection and Immunity

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

    doi:

    Figure Lengend 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.

    Article Snippet: A plasmid library of T. denticola ATCC 35405 genomic DNA was probed for the expression of peptides recognized by antibodies raised against the purified 70-kDa protein (anti-70), and a clone expressing high levels of an immunoreactive 40-kDa peptide was identified.

    Techniques: 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.

    Journal: Infection and Immunity

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

    doi:

    Figure Lengend 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.

    Article Snippet: A plasmid library of T. denticola ATCC 35405 genomic DNA was probed for the expression of peptides recognized by antibodies raised against the purified 70-kDa protein (anti-70), and a clone expressing high levels of an immunoreactive 40-kDa peptide was identified.

    Techniques: Western Blot, Mutagenesis

    Map of the T. denticola opp locus. The 8-kb fragment of T. denticola DNA carried on pMT1 is shown as an open bar, with the locations of some identified restriction enzyme sites shown. Immediately below are arrows representing locations of the genes identified in the opp locus. The solid arrow extending beyond the 8-kb insert represents oppA , while the shaded arrows downstream represent oppB , - C , - D , and - F . Below oppA , the solid arrow represents DNA encoding the 40-kDa LacZ-OppA fusion.

    Journal: Infection and Immunity

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

    doi:

    Figure Lengend Snippet: Map of the T. denticola opp locus. The 8-kb fragment of T. denticola DNA carried on pMT1 is shown as an open bar, with the locations of some identified restriction enzyme sites shown. Immediately below are arrows representing locations of the genes identified in the opp locus. The solid arrow extending beyond the 8-kb insert represents oppA , while the shaded arrows downstream represent oppB , - C , - D , and - F . Below oppA , the solid arrow represents DNA encoding the 40-kDa LacZ-OppA fusion.

    Article Snippet: A plasmid library of T. denticola ATCC 35405 genomic DNA was probed for the expression of peptides recognized by antibodies raised against the purified 70-kDa protein (anti-70), and a clone expressing high levels of an immunoreactive 40-kDa peptide was identified.

    Techniques:

    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.

    Journal: Infection and Immunity

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

    doi:

    Figure Lengend 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.

    Article Snippet: A plasmid library of T. denticola ATCC 35405 genomic DNA was probed for the expression of peptides recognized by antibodies raised against the purified 70-kDa protein (anti-70), and a clone expressing high levels of an immunoreactive 40-kDa peptide was identified.

    Techniques: Southern Blot, Western Blot

    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.

    Journal: Journal of Bacteriology

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

    doi: 10.1128/JB.00528-18

    Figure Lengend 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.

    Article Snippet: As shown in , antibodies to native ATCC 35405 Msp reacted with both intact and permeabilized T. denticola ATCC 35405 cells.

    Techniques: 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.

    Journal: Journal of Bacteriology

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

    doi: 10.1128/JB.00528-18

    Figure Lengend 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.

    Article Snippet: As shown in , antibodies to native ATCC 35405 Msp reacted with both intact and permeabilized T. denticola ATCC 35405 cells.

    Techniques: 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.

    Journal: Journal of Bacteriology

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

    doi: 10.1128/JB.00528-18

    Figure Lengend 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.

    Article Snippet: As shown in , antibodies to native ATCC 35405 Msp reacted with both intact and permeabilized T. denticola ATCC 35405 cells.

    Techniques: Generated

    CGase amino acid sequences from T. denticola strains ATCC 35404 and 35405. The top line in each row shows the predicted amino acid sequence for CGase from strain ATCC 35404 (this paper). The second line ). The asterisks represent amino acids that are identical in the two strains. Triangles ).

    Journal: The Journal of Biological Chemistry

    Article Title: A 52-kDa Leucyl Aminopeptidase from Treponema denticola Is a Cysteinylglycinase That Mediates the Second Step of Glutathione Metabolism *

    doi: 10.1074/jbc.M801034200

    Figure Lengend Snippet: CGase amino acid sequences from T. denticola strains ATCC 35404 and 35405. The top line in each row shows the predicted amino acid sequence for CGase from strain ATCC 35404 (this paper). The second line ). The asterisks represent amino acids that are identical in the two strains. Triangles ).

    Article Snippet: To rectify this, we first showed that sonicated extracts of T. denticola strain ATCC 35404 had CGase activity ( ).

    Techniques: Sequencing

    Fractionation of 52-kDa CGase from T. denticola ATCC 35404 on a HiTrap Q FF column. a , fractions from the separation of a partially purified protein extract on a HiTrap Sepharose Q FF ion exchange column were assayed for CGase activity ( squares ) and total protein ( diamonds , as OD 280 ). b ) of the proteins present in the sample that was loaded onto the ion exchange column ( lane 1 ) and the proteins present in fraction 15 that had the peak CGase activity ( lane 2 ). Proteins of known molecular weight were run in lane MW , and the gel was stained with 0.025% Coomassie Brilliant Blue R-250.

    Journal: The Journal of Biological Chemistry

    Article Title: A 52-kDa Leucyl Aminopeptidase from Treponema denticola Is a Cysteinylglycinase That Mediates the Second Step of Glutathione Metabolism *

    doi: 10.1074/jbc.M801034200

    Figure Lengend Snippet: Fractionation of 52-kDa CGase from T. denticola ATCC 35404 on a HiTrap Q FF column. a , fractions from the separation of a partially purified protein extract on a HiTrap Sepharose Q FF ion exchange column were assayed for CGase activity ( squares ) and total protein ( diamonds , as OD 280 ). b ) of the proteins present in the sample that was loaded onto the ion exchange column ( lane 1 ) and the proteins present in fraction 15 that had the peak CGase activity ( lane 2 ). Proteins of known molecular weight were run in lane MW , and the gel was stained with 0.025% Coomassie Brilliant Blue R-250.

    Article Snippet: To rectify this, we first showed that sonicated extracts of T. denticola strain ATCC 35404 had CGase activity ( ).

    Techniques: Fractionation, Purification, Activity Assay, Molecular Weight, Staining

    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.

    Journal: Infection and Immunity

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

    doi:

    Figure Lengend 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.

    Article Snippet: In the strains in which oppA was detected, the oppA probe hybridized with a 1.1-kb Hin dIII fragment, except that in T. denticola ATCC 35404 the oppA band was 9 kb (Fig. A, lane 2).

    Techniques: Southern Blot, Western Blot

    T. denticola proteases are not responsible for resistance to hβD-2. (A) T. denticola ATCC 35404 incubated in the presence or absence of 100 μM chymostatin (CHY) remained resistant to 10 μg of hβD-2 per ml over a 4-h period. (B) E. coli was incubated in the presence of 10 μg of hβD-2 per ml for 4 h, with or without equal numbers of T. denticola ATCC 35404. Data are means ± SEM from five (A) and three (B) experiments. SDS, sodium dodecyl sulfate.

    Journal: Infection and Immunity

    Article Title: Treponema denticola Is Resistant to Human ?-Defensins

    doi: 10.1128/IAI.70.7.3982-3984.2002

    Figure Lengend Snippet: T. denticola proteases are not responsible for resistance to hβD-2. (A) T. denticola ATCC 35404 incubated in the presence or absence of 100 μM chymostatin (CHY) remained resistant to 10 μg of hβD-2 per ml over a 4-h period. (B) E. coli was incubated in the presence of 10 μg of hβD-2 per ml for 4 h, with or without equal numbers of T. denticola ATCC 35404. Data are means ± SEM from five (A) and three (B) experiments. SDS, sodium dodecyl sulfate.

    Article Snippet: Similar results were seen with 3-day, mid-logarithmic-phase T. denticola ATCC 35404, and no increase in killing of T. denticola was seen even after 24 h of exposure to 100 μg of hβD per ml (data not shown).

    Techniques: Incubation

    Northern blot analyses of the hbpA and hbpB mRNAs. (A) Total RNA was isolated from T. denticola ATCC 35404 grown in GM-1 medium plus 200 μM BPD or in GM-1 medium. The indicated amounts of RNA were separated on a 1% agarose gel and stained with ethidium bromide. (B and C) The RNA was then transferred to a membrane and hybridized with an hbpA probe (a 333-bp Hin dIII fragment internal to the hbpA gene) (B) or an hbpB probe (a PCR product internal to the hbpB gene) (C). Each sample in panel C contained 3 μg of total RNA.

    Journal: Infection and Immunity

    Article Title: Cloning and Expression of Two Novel Hemin Binding Protein Genes from Treponema denticola

    doi: 10.1128/IAI.69.7.4465-4472.2001

    Figure Lengend Snippet: Northern blot analyses of the hbpA and hbpB mRNAs. (A) Total RNA was isolated from T. denticola ATCC 35404 grown in GM-1 medium plus 200 μM BPD or in GM-1 medium. The indicated amounts of RNA were separated on a 1% agarose gel and stained with ethidium bromide. (B and C) The RNA was then transferred to a membrane and hybridized with an hbpA probe (a 333-bp Hin dIII fragment internal to the hbpA gene) (B) or an hbpB probe (a PCR product internal to the hbpB gene) (C). Each sample in panel C contained 3 μg of total RNA.

    Article Snippet: Therefore, Southern blot analysis was performed on genomic DNA isolated from six different T. denticola strains, including ATCC 35405, which is the strain that was used by Scott et al. , and ATCC 33520, which is the strain being sequenced by The Institute for Genomic Research.

    Techniques: Northern Blot, Isolation, Agarose Gel Electrophoresis, Staining, Polymerase Chain Reaction

    (A) Sequences of the noncoding DNA segments around the hbpA and hbpB genes. The dotted lines around a gene name represent the coding region sequences for orf1, hbpA, hbpB , and orf4 . The possible promoter region for hbpA is indicated by −10 and −35. The inverted repeats, which may serve as rho-independent terminators, are marked by pairs of arrows. SD, Shine-Dalgarno site. (B) Comparison of deduced amino acid sequences of HbpA and HbpB from T. denticola . The putative signal peptide sequences are underlined. The asterisks denote positions with identical amino acids in the two proteins. The dashes indicate gaps introduced to maximize the alignment.

    Journal: Infection and Immunity

    Article Title: Cloning and Expression of Two Novel Hemin Binding Protein Genes from Treponema denticola

    doi: 10.1128/IAI.69.7.4465-4472.2001

    Figure Lengend Snippet: (A) Sequences of the noncoding DNA segments around the hbpA and hbpB genes. The dotted lines around a gene name represent the coding region sequences for orf1, hbpA, hbpB , and orf4 . The possible promoter region for hbpA is indicated by −10 and −35. The inverted repeats, which may serve as rho-independent terminators, are marked by pairs of arrows. SD, Shine-Dalgarno site. (B) Comparison of deduced amino acid sequences of HbpA and HbpB from T. denticola . The putative signal peptide sequences are underlined. The asterisks denote positions with identical amino acids in the two proteins. The dashes indicate gaps introduced to maximize the alignment.

    Article Snippet: Therefore, Southern blot analysis was performed on genomic DNA isolated from six different T. denticola strains, including ATCC 35405, which is the strain that was used by Scott et al. , and ATCC 33520, which is the strain being sequenced by The Institute for Genomic Research.

    Techniques:

    Molecular organization of hbpA region from T. denticola strain TD-4. Key restriction endonuclease sites are marked. Inserts pSH2 and pSH5 were cloned into pBluescript. The pSH3, pSH4, and pSH8 inserts were cloned into pUC18. The pSH9 PCR product was cloned into pRsetA.

    Journal: Infection and Immunity

    Article Title: Cloning and Expression of Two Novel Hemin Binding Protein Genes from Treponema denticola

    doi: 10.1128/IAI.69.7.4465-4472.2001

    Figure Lengend Snippet: Molecular organization of hbpA region from T. denticola strain TD-4. Key restriction endonuclease sites are marked. Inserts pSH2 and pSH5 were cloned into pBluescript. The pSH3, pSH4, and pSH8 inserts were cloned into pUC18. The pSH9 PCR product was cloned into pRsetA.

    Article Snippet: Therefore, Southern blot analysis was performed on genomic DNA isolated from six different T. denticola strains, including ATCC 35405, which is the strain that was used by Scott et al. , and ATCC 33520, which is the strain being sequenced by The Institute for Genomic Research.

    Techniques: Clone Assay, Polymerase Chain Reaction

    Characterization of HbpA protein expressed in E. coli . (A) Total protein samples were prepared from the cells indicated and separated by SDS-PAGE before being transferred to a nylon membrane. The primary antibody used in the subsequent Western blotting was anti-HbpA antiserum prepared previously against HbpA purified from T. denticola . Lanes: 1, molecular size standards; 2, protein from E. coli DH5α with pBluescript vector alone; 3, protein from E. coli DH5α with pSH5; 4, OMP from T. denticola grown in GM-1 plus 200 μM BPD. (B) Various protein samples were subjected to LDS-PAGE and stained with Coomassie brilliant blue. Lanes: 1, prestained molecular size standards; 2, 250 ng of purified rHbpA from E. coli ; 3, 10 μg of OMP from T. denticola grown in GM-1 medium; 4, 10 μg of OMP from T. denticola grown in GM-1 plus 200 μM BPD. (C) The indicated protein samples were subjected to LDS-PAGE and reacted with TMBZ. Lanes: 1, prestained molecular size standards; 2, 250 ng of purified rHbpA not treated with hemin; 3, 250 ng of purified rHbpA preincubated with hemin; 4, 10 μg of OMP from T. denticola grown in GM-1 medium and then preincubated with hemin; 5, 10 μg of OMP from T. denticola grown in GM-1 plus 200 μM BPD and then preincubated with hemin. The position of the 44-kDa HbpA protein is marked by an arrow.

    Journal: Infection and Immunity

    Article Title: Cloning and Expression of Two Novel Hemin Binding Protein Genes from Treponema denticola

    doi: 10.1128/IAI.69.7.4465-4472.2001

    Figure Lengend Snippet: Characterization of HbpA protein expressed in E. coli . (A) Total protein samples were prepared from the cells indicated and separated by SDS-PAGE before being transferred to a nylon membrane. The primary antibody used in the subsequent Western blotting was anti-HbpA antiserum prepared previously against HbpA purified from T. denticola . Lanes: 1, molecular size standards; 2, protein from E. coli DH5α with pBluescript vector alone; 3, protein from E. coli DH5α with pSH5; 4, OMP from T. denticola grown in GM-1 plus 200 μM BPD. (B) Various protein samples were subjected to LDS-PAGE and stained with Coomassie brilliant blue. Lanes: 1, prestained molecular size standards; 2, 250 ng of purified rHbpA from E. coli ; 3, 10 μg of OMP from T. denticola grown in GM-1 medium; 4, 10 μg of OMP from T. denticola grown in GM-1 plus 200 μM BPD. (C) The indicated protein samples were subjected to LDS-PAGE and reacted with TMBZ. Lanes: 1, prestained molecular size standards; 2, 250 ng of purified rHbpA not treated with hemin; 3, 250 ng of purified rHbpA preincubated with hemin; 4, 10 μg of OMP from T. denticola grown in GM-1 medium and then preincubated with hemin; 5, 10 μg of OMP from T. denticola grown in GM-1 plus 200 μM BPD and then preincubated with hemin. The position of the 44-kDa HbpA protein is marked by an arrow.

    Article Snippet: Therefore, Southern blot analysis was performed on genomic DNA isolated from six different T. denticola strains, including ATCC 35405, which is the strain that was used by Scott et al. , and ATCC 33520, which is the strain being sequenced by The Institute for Genomic Research.

    Techniques: SDS Page, Western Blot, Purification, Plasmid Preparation, Polyacrylamide Gel Electrophoresis, Staining

    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: HGF challenge with several strains of T. denticola and the OM extract of T. denticola ATCC 35405 resulted in a diminished accumulation of radiolabeled IPs relative to both 15 and 1% fetal bovine serum, which served as strongly positive and background control agonists, respectively.

    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: HGF challenge with several strains of T. denticola and the OM extract of T. denticola ATCC 35405 resulted in a diminished accumulation of radiolabeled IPs relative to both 15 and 1% fetal bovine serum, which served as strongly positive and background control agonists, respectively.

    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: HGF challenge with several strains of T. denticola and the OM extract of T. denticola ATCC 35405 resulted in a diminished accumulation of radiolabeled IPs relative to both 15 and 1% fetal bovine serum, which served as strongly positive and background control agonists, respectively.

    Techniques: SDS Page, Nucleic Acid Electrophoresis