t. denticola Search Results


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  • 99
    ATCC t denticola
    Oral microbiota levels in the subgingival plaque from elderly individuals with periodontal health ( n = 17), gingivitis ( n = 19), and chronic periodontitis ( n = 15). The individual values represent bacterial counts per sample in the subgingival plaque ( a ) Total bacterial counts, ( b ) F. nucleatum , ( c ) P. intermedia , ( d ) P. gingivalis , ( e ) T. <t>denticola</t> , and ( f ) T. forsythia . The horizontal lines in the middle of the box represent the median and whiskers are drawn down to the 10 th through 90 th percentiles. The points below and above the whiskers are drawn as individual dots
    T Denticola, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 387 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore total t denticola rna
    T. <t>denticola</t> tro operon is negatively regulated by Mn 2+ and Fe 2+ . Expression of troA was analysed by qRT-PCR. <t>RNA</t> extracted from T. denticola grown in NOS-EC media supplemented with 5 μM Fe 2+ , Mn 2+ or Zn 2+ was quantified at (A) 24 h or (B) 48 h post inoculation using specific primers and probes with the Taqman system. Values have been normalized to the internal control, flaA . Fold changes are relative to spirochaetes grown in NOS-EC media lacking metal supplmentation (control). Results represent the means and standard deviations of three independent experiments performed in quadruplicate.
    Total T Denticola Rna, supplied by Millipore, 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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    97
    ATCC t denticola motility mutants t denticola atcc 33520 motility mutants
    Characterization of T. <t>denticola</t> wild-type, Δ flgE , Δ motB . (A) Growth of T. denticola wild-type and mutants. T. denticola cultures at stationary phase were inoculated into fresh OBGM medium at t = 0. A 650 of the cultures was measured at 6–24 h intervals for 264 h. The mean generation time was calculated based on the rate of change of A 650 during the exponential growth phase of cultures ( N = 3). The mean generation times were statistically analyzed using a one way ANOVA with both mutants Δ motB and Δ flgE significantly different ( p
    T Denticola Motility Mutants T Denticola Atcc 33520 Motility Mutants, supplied by ATCC, used in various techniques. Bioz Stars score: 97/100, based on 18 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    DSMZ t denticola dsm14222 genomic dna
    Characterization of T. <t>denticola</t> wild-type, Δ flgE , Δ motB . (A) Growth of T. denticola wild-type and mutants. T. denticola cultures at stationary phase were inoculated into fresh OBGM medium at t = 0. A 650 of the cultures was measured at 6–24 h intervals for 264 h. The mean generation time was calculated based on the rate of change of A 650 during the exponential growth phase of cultures ( N = 3). The mean generation times were statistically analyzed using a one way ANOVA with both mutants Δ motB and Δ flgE significantly different ( p
    T Denticola Dsm14222 Genomic Dna, supplied by DSMZ, used in various techniques. Bioz Stars score: 90/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Softberry Inc t denticola genome sequence
    Interaction of PrcB with PrtP. Arrows denote PrcB, PrtP, and rabbit IgG heavy chains (H). (A) Immunoblots probed with anti-PrtP antibodies and HisProbe reagent, as indicated. Lanes 1 and 2, T. <t>denticola</t> CF499; lanes 3 and 4, CF417; lanes 1 and 4, cell extracts; lanes 2 and 3, anti-PrtP immunoprecipitates from cell extracts. (B) T. denticola CF499 lysates were immunoprecipitated with polyclonal antibodies to PrtP, PrcA, FlaA, or Msp. Eluted proteins on duplicate blots were probed with anti-PrtP antibodies and HisProbe reagent, as indicated. (C) Immunoblot probed with anti-PrtP antibodies. Lanes 1 to 3, T. denticola CF499; lanes 4 to 6, T. denticola CF417; lanes 1 and 4, whole-cell extracts; lanes 2 and 5, anti-6×His monoclonal antibody immunoprecipitates from cell extracts; lanes 3 and 6, anti-PrtP antibody immunoprecipitates from cell extracts. (D) E. coli cells expressing PrtP, 6×His-PrcB, or both PrtP and 6×His-PrcB were analyzed directly and after Ni 2+ chromatography. Immunoblots of whole-cell extracts and Ni 2+ affinity column eluates were probed with anti-6×His monoclonal antibody or anti-PrtP polyclonal antibodies. Lanes: 1, E. coli /pCF411 (expresses PrtP); 2, E. coli /pCF415 (expresses PrcB-6×His); 3, E. coli /pCF416 (expresses PrcB-6×His + PrtP).
    T Denticola Genome Sequence, supplied by Softberry Inc, used in various techniques. Bioz Stars score: 85/100, based on 14 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    ATCC t denticola atcc strains
    Northern blot analyses of the hbpA and hbpB mRNAs. (A) Total RNA was isolated from T. <t>denticola</t> <t>ATCC</t> 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 Atcc Strains, supplied by ATCC, used in various techniques. Bioz Stars score: 91/100, based on 27 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Alpha Diagnostics t denticola membrane fraction
    Cytotoxic effects of T. <t>denticola</t> on human gingival fibroblasts. The cultured hGF cells were challenged by T. denticola and were viewed by phase-contrast microscopy after 48 h. A. Unchallenged cells serve as negative control. B. hGF cells challenged with wildtype manifested a rounded shape. C. hGF cells challenged with fbp mutant showed less morphologic changes than those infected with wildtype. D. Survival of hGF cells were determined 5 days after challenge with T. denticola . The fbp mutant caused less cell death at concentration of 0.37 × 10 8 and 1.1 × 10 8 (*P
    T Denticola Membrane Fraction, supplied by Alpha Diagnostics, used in various techniques. Bioz Stars score: 88/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    ATCC t denticola atcc 35404
    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. <t>denticola</t> 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.
    T Denticola Atcc 35404, supplied by ATCC, used in various techniques. Bioz Stars score: 94/100, based on 136 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    ATCC t denticola atcc 34505
    A phylogenetic split in spirochete mode of growth. ( A – D ) Cultures of spirochetes from different genera were incubated with variable concentrations of HADA for 30 min and analyzed at the single-cell level in a demograph. Heat map displays the relative fluorescence intensity in arbitrary units (0–1). ( A ) Borrelia miyamotoi strain LS-2000, 0.1 mM HADA, n = 173. ( B ) B. hermsii , 0.1 mM HADA, n = 391. ( C ) T. <t>denticola</t> ATCC 34505, 0.2 mM HADA, n = 2132. ( D ) L. interrogans serovar Conpenhageni strain Fiocruz L1-130, 0.4 mM HADA, n = 373. ( E ) Bar graphs depicting the percent of cells with a given number of zones.
    T Denticola Atcc 34505, supplied by ATCC, used in various techniques. Bioz Stars score: 90/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    ATCC t denticola atcc 700768
    A phylogenetic split in spirochete mode of growth. ( A – D ) Cultures of spirochetes from different genera were incubated with variable concentrations of HADA for 30 min and analyzed at the single-cell level in a demograph. Heat map displays the relative fluorescence intensity in arbitrary units (0–1). ( A ) Borrelia miyamotoi strain LS-2000, 0.1 mM HADA, n = 173. ( B ) B. hermsii , 0.1 mM HADA, n = 391. ( C ) T. <t>denticola</t> ATCC 34505, 0.2 mM HADA, n = 2132. ( D ) L. interrogans serovar Conpenhageni strain Fiocruz L1-130, 0.4 mM HADA, n = 373. ( E ) Bar graphs depicting the percent of cells with a given number of zones.
    T Denticola Atcc 700768, supplied by ATCC, used in various techniques. Bioz Stars score: 92/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    ATCC t denticola atcc 33405
    A phylogenetic split in spirochete mode of growth. ( A – D ) Cultures of spirochetes from different genera were incubated with variable concentrations of HADA for 30 min and analyzed at the single-cell level in a demograph. Heat map displays the relative fluorescence intensity in arbitrary units (0–1). ( A ) Borrelia miyamotoi strain LS-2000, 0.1 mM HADA, n = 173. ( B ) B. hermsii , 0.1 mM HADA, n = 391. ( C ) T. <t>denticola</t> ATCC 34505, 0.2 mM HADA, n = 2132. ( D ) L. interrogans serovar Conpenhageni strain Fiocruz L1-130, 0.4 mM HADA, n = 373. ( E ) Bar graphs depicting the percent of cells with a given number of zones.
    T Denticola Atcc 33405, supplied by ATCC, used in various techniques. Bioz Stars score: 85/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Oral microbiota levels in the subgingival plaque from elderly individuals with periodontal health ( n = 17), gingivitis ( n = 19), and chronic periodontitis ( n = 15). The individual values represent bacterial counts per sample in the subgingival plaque ( a ) Total bacterial counts, ( b ) F. nucleatum , ( c ) P. intermedia , ( d ) P. gingivalis , ( e ) T. denticola , and ( f ) T. forsythia . The horizontal lines in the middle of the box represent the median and whiskers are drawn down to the 10 th through 90 th percentiles. The points below and above the whiskers are drawn as individual dots

    Journal: BMC Infectious Diseases

    Article Title: Impact of aging on TREM-1 responses in the periodontium: a cross-sectional study in an elderly population

    doi: 10.1186/s12879-016-1778-6

    Figure Lengend Snippet: Oral microbiota levels in the subgingival plaque from elderly individuals with periodontal health ( n = 17), gingivitis ( n = 19), and chronic periodontitis ( n = 15). The individual values represent bacterial counts per sample in the subgingival plaque ( a ) Total bacterial counts, ( b ) F. nucleatum , ( c ) P. intermedia , ( d ) P. gingivalis , ( e ) T. denticola , and ( f ) T. forsythia . The horizontal lines in the middle of the box represent the median and whiskers are drawn down to the 10 th through 90 th percentiles. The points below and above the whiskers are drawn as individual dots

    Article Snippet: T. forsythia (OMZ 1047), T. denticola (ATCC 35405; OMZ 661), P. intermedia (OMZ 278), F. nucleatum (OMZ 598), were maintained in liquid cultures as described earlier [ ].

    Techniques:

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

    Journal: Applied and Environmental Microbiology

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

    doi: 10.1128/AEM.00417-11

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

    Article Snippet: Briefly, three T. denticola strains (ATCC 35405, ATCC 33520, and the TDE0911 mutant) were grown to early logarithmic phase (optical density at 600 nm of 0.3 to 0.4), and the cells were enumerated using Petroff-Hausser counting chambers.

    Techniques: Transformation Assay, Methylation, Plasmid Preparation, Mutagenesis

    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

    Effect of dissipation of proton motive force on total association of β-defensins with T. denticola . A total of 1 × 10 8 cells/ml of T. denticola 35404 were incubated with biotinylated β-defensin 2 or 3 (10 μg/ml) and 50

    Journal:

    Article Title: Mechanisms of Decreased Susceptibility to ?-Defensins by Treponema denticola ▿

    doi: 10.1128/IAI.01718-06

    Figure Lengend Snippet: Effect of dissipation of proton motive force on total association of β-defensins with T. denticola . A total of 1 × 10 8 cells/ml of T. denticola 35404 were incubated with biotinylated β-defensin 2 or 3 (10 μg/ml) and 50

    Article Snippet: An analysis of the T. denticola genome (ATCC 35405) indicated that there is a lack of LPS structural genes ( ).

    Techniques: Incubation

    Dissipation of proton motive force increases T. denticola sensitivity to hβD-3. (A) A total of 1 × 10 8 cells/ml of T. denticola 35404 were incubated in triplicate at 37°C with 35 μM CCCP or DMSO (solvent). Then 10 μl/well

    Journal:

    Article Title: Mechanisms of Decreased Susceptibility to ?-Defensins by Treponema denticola ▿

    doi: 10.1128/IAI.01718-06

    Figure Lengend Snippet: Dissipation of proton motive force increases T. denticola sensitivity to hβD-3. (A) A total of 1 × 10 8 cells/ml of T. denticola 35404 were incubated in triplicate at 37°C with 35 μM CCCP or DMSO (solvent). Then 10 μl/well

    Article Snippet: An analysis of the T. denticola genome (ATCC 35405) indicated that there is a lack of LPS structural genes ( ).

    Techniques: Incubation

    (A) Binding of biotinylated β-defensin 2 to bacteria. A total of 1 × 10 8 cells/ml of T. denticola (Td) strains cultured in GM-1 medium, E. coli , or S. aureus 113 dlt were incubated in triplicate with biotinylated β-defensin 2 (10

    Journal:

    Article Title: Mechanisms of Decreased Susceptibility to ?-Defensins by Treponema denticola ▿

    doi: 10.1128/IAI.01718-06

    Figure Lengend Snippet: (A) Binding of biotinylated β-defensin 2 to bacteria. A total of 1 × 10 8 cells/ml of T. denticola (Td) strains cultured in GM-1 medium, E. coli , or S. aureus 113 dlt were incubated in triplicate with biotinylated β-defensin 2 (10

    Article Snippet: An analysis of the T. denticola genome (ATCC 35405) indicated that there is a lack of LPS structural genes ( ).

    Techniques: Binding Assay, Cell Culture, Incubation

    Effect of host proteins present in the growth medium on T. denticola susceptibility to β-defensins. A total of 1 × 10 5 T. denticola 35404 cells grown in GM-1 serum-containing medium or in chemically defined medium (CDM) lacking serum,

    Journal:

    Article Title: Mechanisms of Decreased Susceptibility to ?-Defensins by Treponema denticola ▿

    doi: 10.1128/IAI.01718-06

    Figure Lengend Snippet: Effect of host proteins present in the growth medium on T. denticola susceptibility to β-defensins. A total of 1 × 10 5 T. denticola 35404 cells grown in GM-1 serum-containing medium or in chemically defined medium (CDM) lacking serum,

    Article Snippet: An analysis of the T. denticola genome (ATCC 35405) indicated that there is a lack of LPS structural genes ( ).

    Techniques:

    (A) Binding of biotinylated β-defensin 3 to bacteria. A total of 1 × 10 8 cells/ml of T. denticola (Td) strains cultured in GM-1, E. coli , or S. aureus 113 dlt were incubated in triplicate with biotinylated β-defensin-3 (10 μg/ml)

    Journal:

    Article Title: Mechanisms of Decreased Susceptibility to ?-Defensins by Treponema denticola ▿

    doi: 10.1128/IAI.01718-06

    Figure Lengend Snippet: (A) Binding of biotinylated β-defensin 3 to bacteria. A total of 1 × 10 8 cells/ml of T. denticola (Td) strains cultured in GM-1, E. coli , or S. aureus 113 dlt were incubated in triplicate with biotinylated β-defensin-3 (10 μg/ml)

    Article Snippet: An analysis of the T. denticola genome (ATCC 35405) indicated that there is a lack of LPS structural genes ( ).

    Techniques: Binding Assay, Cell Culture, Incubation

    Quenching of a fluorescent dye in the presence of efflux pump inhibitors. A total of 1 × 10 8 cells/ml of T. denticola 35404 were incubated in 12 replicates at 37°C with 10 μg/ml reserpine, 20 μg/ml verapamil, 50 μM

    Journal:

    Article Title: Mechanisms of Decreased Susceptibility to ?-Defensins by Treponema denticola ▿

    doi: 10.1128/IAI.01718-06

    Figure Lengend Snippet: Quenching of a fluorescent dye in the presence of efflux pump inhibitors. A total of 1 × 10 8 cells/ml of T. denticola 35404 were incubated in 12 replicates at 37°C with 10 μg/ml reserpine, 20 μg/ml verapamil, 50 μM

    Article Snippet: An analysis of the T. denticola genome (ATCC 35405) indicated that there is a lack of LPS structural genes ( ).

    Techniques: Incubation

    Silver-stained polyacrylamide gel of purified native ATCC 35405 Msp. Lane 1, unheated sample; lane 2, boiled sample. Arrows indicate oligomeric Msp (lane 1, 150 to 200 kDa) and monomeric Msp (lane 2, approximately 53 kDa). This preparation was used to raise rabbit antibodies against native Msp.

    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: Silver-stained polyacrylamide gel of purified native ATCC 35405 Msp. Lane 1, unheated sample; lane 2, boiled sample. Arrows indicate oligomeric Msp (lane 1, 150 to 200 kDa) and monomeric Msp (lane 2, approximately 53 kDa). This preparation was used to raise rabbit antibodies against native Msp.

    Article Snippet: First, we identified a surface-exposed epitope of T. denticola ATCC 35405 Msp within a 23-residue domain in the central region of the protein that lies between the predicted Msp N-terminal (pfam02707, residues 109 to 208) and C-terminal (pfam02722, residues 360 to 543) domains.

    Techniques: Staining, Purification

    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: First, we identified a surface-exposed epitope of T. denticola ATCC 35405 Msp within a 23-residue domain in the central region of the protein that lies between the predicted Msp N-terminal (pfam02707, residues 109 to 208) and C-terminal (pfam02722, residues 360 to 543) domains.

    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: First, we identified a surface-exposed epitope of T. denticola ATCC 35405 Msp within a 23-residue domain in the central region of the protein that lies between the predicted Msp N-terminal (pfam02707, residues 109 to 208) and C-terminal (pfam02722, residues 360 to 543) domains.

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

    Alignment of the Msp central domains of strains ATCC 35405 and ATCC 33520. Amino acid residue numbers are shown at the sequence ends. Purple-highlighted residues represent areas of high predicted antigenic index values (Ag1 and Ag2). Green-highlighted residues represent approximate boundaries of the central domain (D1 and D2). Blue-highlighted residues represent the region of greatest difference between the Msps other than Ag1 and Ag2 (Xr). Other than the region shown here, the amino acid sequences of the two proteins are identical, with 543 and 547 residues, respectively.

    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: Alignment of the Msp central domains of strains ATCC 35405 and ATCC 33520. Amino acid residue numbers are shown at the sequence ends. Purple-highlighted residues represent areas of high predicted antigenic index values (Ag1 and Ag2). Green-highlighted residues represent approximate boundaries of the central domain (D1 and D2). Blue-highlighted residues represent the region of greatest difference between the Msps other than Ag1 and Ag2 (Xr). Other than the region shown here, the amino acid sequences of the two proteins are identical, with 543 and 547 residues, respectively.

    Article Snippet: First, we identified a surface-exposed epitope of T. denticola ATCC 35405 Msp within a 23-residue domain in the central region of the protein that lies between the predicted Msp N-terminal (pfam02707, residues 109 to 208) and C-terminal (pfam02722, residues 360 to 543) domains.

    Techniques: Sequencing

    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: First, we identified a surface-exposed epitope of T. denticola ATCC 35405 Msp within a 23-residue domain in the central region of the protein that lies between the predicted Msp N-terminal (pfam02707, residues 109 to 208) and C-terminal (pfam02722, residues 360 to 543) domains.

    Techniques: Generated

    T. denticola tro operon is negatively regulated by Mn 2+ and Fe 2+ . Expression of troA was analysed by qRT-PCR. RNA extracted from T. denticola grown in NOS-EC media supplemented with 5 μM Fe 2+ , Mn 2+ or Zn 2+ was quantified at (A) 24 h or (B) 48 h post inoculation using specific primers and probes with the Taqman system. Values have been normalized to the internal control, flaA . Fold changes are relative to spirochaetes grown in NOS-EC media lacking metal supplmentation (control). Results represent the means and standard deviations of three independent experiments performed in quadruplicate.

    Journal: Molecular Microbiology

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

    doi: 10.1111/j.1365-2958.2008.06418.x

    Figure Lengend Snippet: T. denticola tro operon is negatively regulated by Mn 2+ and Fe 2+ . Expression of troA was analysed by qRT-PCR. RNA extracted from T. denticola grown in NOS-EC media supplemented with 5 μM Fe 2+ , Mn 2+ or Zn 2+ was quantified at (A) 24 h or (B) 48 h post inoculation using specific primers and probes with the Taqman system. Values have been normalized to the internal control, flaA . Fold changes are relative to spirochaetes grown in NOS-EC media lacking metal supplmentation (control). Results represent the means and standard deviations of three independent experiments performed in quadruplicate.

    Article Snippet: Briefly, T. denticola RNA was extracted using TRI-Reagent (Sigma) as described by the manufacturer.

    Techniques: Expressing, Quantitative RT-PCR

    Characterization of T. denticola wild-type, Δ flgE , Δ motB . (A) Growth of T. denticola wild-type and mutants. T. denticola cultures at stationary phase were inoculated into fresh OBGM medium at t = 0. A 650 of the cultures was measured at 6–24 h intervals for 264 h. The mean generation time was calculated based on the rate of change of A 650 during the exponential growth phase of cultures ( N = 3). The mean generation times were statistically analyzed using a one way ANOVA with both mutants Δ motB and Δ flgE significantly different ( p

    Journal: Frontiers in Cellular and Infection Microbiology

    Article Title: The Role of Treponema denticola Motility in Synergistic Biofilm Formation With Porphyromonas gingivalis

    doi: 10.3389/fcimb.2019.00432

    Figure Lengend Snippet: Characterization of T. denticola wild-type, Δ flgE , Δ motB . (A) Growth of T. denticola wild-type and mutants. T. denticola cultures at stationary phase were inoculated into fresh OBGM medium at t = 0. A 650 of the cultures was measured at 6–24 h intervals for 264 h. The mean generation time was calculated based on the rate of change of A 650 during the exponential growth phase of cultures ( N = 3). The mean generation times were statistically analyzed using a one way ANOVA with both mutants Δ motB and Δ flgE significantly different ( p

    Article Snippet: Construction of T. denticola Motility Mutants T. denticola ATCC 33520 motility mutants were constructed where the open reading frame of flgE and motB were deleted.

    Techniques:

    Coaggregation and biofilm formation of T. denticola wild-type, Δ flgE , Δ motB with P. gingivalis W50. (A) Coaggregation of T. denticola wild-type and mutants with P. gingivalis W50. T. denticola ATCC 33520 and P. gingivalis cells at exponential growth phase were harvested, washed twice with coaggregation buffer and adjusted to A 650 of 0.5 with the coaggregation buffer. Equal volumes of T. denticola and P. gingivalis cell suspensions were combined. The height of bacterial aggregates was monitored for 7 h. The data are presented as means plus standard deviations ( N = 3). (B) Monospecies and dual-species static biofilms of T. denticola ATCC 33520 wild-type, Δ flgE , Δ motB with P. gingivalis W50. T. denticola and P. gingivalis cells were grown to exponential phase, diluted to A 650 of 0.15 and grown anaerobically for 5 days in a 12-well plate, either in a monospecies or dual-species culture. The resultant biofilm was stained with crystal violet and the total biomass determined spectrophotometrically. The data are presented as means and standard deviations ( N = 23–27) and were analyzed using a Kruskal-Wallis with Conover-Imam test. All values were significantly different ( p

    Journal: Frontiers in Cellular and Infection Microbiology

    Article Title: The Role of Treponema denticola Motility in Synergistic Biofilm Formation With Porphyromonas gingivalis

    doi: 10.3389/fcimb.2019.00432

    Figure Lengend Snippet: Coaggregation and biofilm formation of T. denticola wild-type, Δ flgE , Δ motB with P. gingivalis W50. (A) Coaggregation of T. denticola wild-type and mutants with P. gingivalis W50. T. denticola ATCC 33520 and P. gingivalis cells at exponential growth phase were harvested, washed twice with coaggregation buffer and adjusted to A 650 of 0.5 with the coaggregation buffer. Equal volumes of T. denticola and P. gingivalis cell suspensions were combined. The height of bacterial aggregates was monitored for 7 h. The data are presented as means plus standard deviations ( N = 3). (B) Monospecies and dual-species static biofilms of T. denticola ATCC 33520 wild-type, Δ flgE , Δ motB with P. gingivalis W50. T. denticola and P. gingivalis cells were grown to exponential phase, diluted to A 650 of 0.15 and grown anaerobically for 5 days in a 12-well plate, either in a monospecies or dual-species culture. The resultant biofilm was stained with crystal violet and the total biomass determined spectrophotometrically. The data are presented as means and standard deviations ( N = 23–27) and were analyzed using a Kruskal-Wallis with Conover-Imam test. All values were significantly different ( p

    Article Snippet: Construction of T. denticola Motility Mutants T. denticola ATCC 33520 motility mutants were constructed where the open reading frame of flgE and motB were deleted.

    Techniques: Staining

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

    Journal: Applied and Environmental Microbiology

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

    doi: 10.1128/AEM.00417-11

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

    Article Snippet: T. denticola ATCC 33520 shares more than 76% DNA similarity with ATCC 35405 ( ).

    Techniques: Transformation Assay, Methylation, Plasmid Preparation, Mutagenesis

    Interaction of PrcB with PrtP. Arrows denote PrcB, PrtP, and rabbit IgG heavy chains (H). (A) Immunoblots probed with anti-PrtP antibodies and HisProbe reagent, as indicated. Lanes 1 and 2, T. denticola CF499; lanes 3 and 4, CF417; lanes 1 and 4, cell extracts; lanes 2 and 3, anti-PrtP immunoprecipitates from cell extracts. (B) T. denticola CF499 lysates were immunoprecipitated with polyclonal antibodies to PrtP, PrcA, FlaA, or Msp. Eluted proteins on duplicate blots were probed with anti-PrtP antibodies and HisProbe reagent, as indicated. (C) Immunoblot probed with anti-PrtP antibodies. Lanes 1 to 3, T. denticola CF499; lanes 4 to 6, T. denticola CF417; lanes 1 and 4, whole-cell extracts; lanes 2 and 5, anti-6×His monoclonal antibody immunoprecipitates from cell extracts; lanes 3 and 6, anti-PrtP antibody immunoprecipitates from cell extracts. (D) E. coli cells expressing PrtP, 6×His-PrcB, or both PrtP and 6×His-PrcB were analyzed directly and after Ni 2+ chromatography. Immunoblots of whole-cell extracts and Ni 2+ affinity column eluates were probed with anti-6×His monoclonal antibody or anti-PrtP polyclonal antibodies. Lanes: 1, E. coli /pCF411 (expresses PrtP); 2, E. coli /pCF415 (expresses PrcB-6×His); 3, E. coli /pCF416 (expresses PrcB-6×His + PrtP).

    Journal: Journal of Bacteriology

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

    doi: 10.1128/JB.00274-10

    Figure Lengend Snippet: Interaction of PrcB with PrtP. Arrows denote PrcB, PrtP, and rabbit IgG heavy chains (H). (A) Immunoblots probed with anti-PrtP antibodies and HisProbe reagent, as indicated. Lanes 1 and 2, T. denticola CF499; lanes 3 and 4, CF417; lanes 1 and 4, cell extracts; lanes 2 and 3, anti-PrtP immunoprecipitates from cell extracts. (B) T. denticola CF499 lysates were immunoprecipitated with polyclonal antibodies to PrtP, PrcA, FlaA, or Msp. Eluted proteins on duplicate blots were probed with anti-PrtP antibodies and HisProbe reagent, as indicated. (C) Immunoblot probed with anti-PrtP antibodies. Lanes 1 to 3, T. denticola CF499; lanes 4 to 6, T. denticola CF417; lanes 1 and 4, whole-cell extracts; lanes 2 and 5, anti-6×His monoclonal antibody immunoprecipitates from cell extracts; lanes 3 and 6, anti-PrtP antibody immunoprecipitates from cell extracts. (D) E. coli cells expressing PrtP, 6×His-PrcB, or both PrtP and 6×His-PrcB were analyzed directly and after Ni 2+ chromatography. Immunoblots of whole-cell extracts and Ni 2+ affinity column eluates were probed with anti-6×His monoclonal antibody or anti-PrtP polyclonal antibodies. Lanes: 1, E. coli /pCF411 (expresses PrtP); 2, E. coli /pCF415 (expresses PrcB-6×His); 3, E. coli /pCF416 (expresses PrcB-6×His + PrtP).

    Article Snippet: Counting from the first AUG codon in the ORF, the deduced amino acid sequences are identical for residues 1 to 65, which includes the predicted untranslated region upstream of the GUG translation initiation codon in the annotated T. denticola genome sequence ( ).

    Techniques: Western Blot, Immunoprecipitation, Expressing, Chromatography, Affinity Column

    Protease locus in T. denticola parent and prcB mutant strains. The genes of the protease operon, prcB , prcA , and prtP , are shown as gray arrows. The location of the protease operon promoter region is indicated by “P.” The protease mRNA transcript is shown as a thin arrow above the genes transcribed in each strain. The location and orientation of the erm cassette are shown by a black arrow. The T. denticola strains are 35405 (wild-type parent), P0760 ( erm insertion at the 5′ end of prcB ), CF417 ( prcB modified to encode a C-terminal His tag; erm insertion replaces the 5′ end of prcA ), CF499 ( prcB modified to encode a C-terminal His tag; erm insertion is upstream of the protease locus), and CF522 (Δ prcB ; promoter region is intact; erm insertion as in CF499).

    Journal: Journal of Bacteriology

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

    doi: 10.1128/JB.00274-10

    Figure Lengend Snippet: Protease locus in T. denticola parent and prcB mutant strains. The genes of the protease operon, prcB , prcA , and prtP , are shown as gray arrows. The location of the protease operon promoter region is indicated by “P.” The protease mRNA transcript is shown as a thin arrow above the genes transcribed in each strain. The location and orientation of the erm cassette are shown by a black arrow. The T. denticola strains are 35405 (wild-type parent), P0760 ( erm insertion at the 5′ end of prcB ), CF417 ( prcB modified to encode a C-terminal His tag; erm insertion replaces the 5′ end of prcA ), CF499 ( prcB modified to encode a C-terminal His tag; erm insertion is upstream of the protease locus), and CF522 (Δ prcB ; promoter region is intact; erm insertion as in CF499).

    Article Snippet: Counting from the first AUG codon in the ORF, the deduced amino acid sequences are identical for residues 1 to 65, which includes the predicted untranslated region upstream of the GUG translation initiation codon in the annotated T. denticola genome sequence ( ).

    Techniques: Mutagenesis, Modification

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

    Journal: Journal of Bacteriology

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

    doi: 10.1128/JB.00274-10

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

    Article Snippet: Counting from the first AUG codon in the ORF, the deduced amino acid sequences are identical for residues 1 to 65, which includes the predicted untranslated region upstream of the GUG translation initiation codon in the annotated T. denticola genome sequence ( ).

    Techniques: Sequencing

    Expression and localization of PrcB. PrcB-6×His and PrtP were detected on blots by use of HisProbe reagent and anti-PrtP antibodies, respectively. Triton X-114 extracts (TX-114) were partitioned into aqueous (Aq) and detergent (Det) phases. Molecular mass standards are shown in panels B and C. (A) Expression of PrcB-6×His detected in lysates of E. coli /pCF415 ( E.c. ) and T. denticola strains CF499 and CF417. (B) PrcB-6×His localizes to the detergent phase of a T. denticola CF499 Triton X-114 extract. (C) T. denticola CF499 Triton X-114 extract showing differential phase partitioning of full-length and N-terminally truncated PrcB-6×His. Samples were heated (+) or not heated (−) prior to SDS-PAGE.

    Journal: Journal of Bacteriology

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

    doi: 10.1128/JB.00274-10

    Figure Lengend Snippet: Expression and localization of PrcB. PrcB-6×His and PrtP were detected on blots by use of HisProbe reagent and anti-PrtP antibodies, respectively. Triton X-114 extracts (TX-114) were partitioned into aqueous (Aq) and detergent (Det) phases. Molecular mass standards are shown in panels B and C. (A) Expression of PrcB-6×His detected in lysates of E. coli /pCF415 ( E.c. ) and T. denticola strains CF499 and CF417. (B) PrcB-6×His localizes to the detergent phase of a T. denticola CF499 Triton X-114 extract. (C) T. denticola CF499 Triton X-114 extract showing differential phase partitioning of full-length and N-terminally truncated PrcB-6×His. Samples were heated (+) or not heated (−) prior to SDS-PAGE.

    Article Snippet: Counting from the first AUG codon in the ORF, the deduced amino acid sequences are identical for residues 1 to 65, which includes the predicted untranslated region upstream of the GUG translation initiation codon in the annotated T. denticola genome sequence ( ).

    Techniques: Expressing, SDS Page

    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: Southern blot analysis demonstrated that hbpA is present in several T. denticola ATCC strains and clinical isolates, but not in Treponema pectinovorum, Treponema socranskii , or Escherichia coli .

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

    Cytotoxic effects of T. denticola on human gingival fibroblasts. The cultured hGF cells were challenged by T. denticola and were viewed by phase-contrast microscopy after 48 h. A. Unchallenged cells serve as negative control. B. hGF cells challenged with wildtype manifested a rounded shape. C. hGF cells challenged with fbp mutant showed less morphologic changes than those infected with wildtype. D. Survival of hGF cells were determined 5 days after challenge with T. denticola . The fbp mutant caused less cell death at concentration of 0.37 × 10 8 and 1.1 × 10 8 (*P

    Journal: Anaerobe

    Article Title: Fibronectin-binding protein TDE1579 affects cytotoxicity of Treponema denticola

    doi: 10.1016/j.anaerobe.2015.09.010

    Figure Lengend Snippet: Cytotoxic effects of T. denticola on human gingival fibroblasts. The cultured hGF cells were challenged by T. denticola and were viewed by phase-contrast microscopy after 48 h. A. Unchallenged cells serve as negative control. B. hGF cells challenged with wildtype manifested a rounded shape. C. hGF cells challenged with fbp mutant showed less morphologic changes than those infected with wildtype. D. Survival of hGF cells were determined 5 days after challenge with T. denticola . The fbp mutant caused less cell death at concentration of 0.37 × 10 8 and 1.1 × 10 8 (*P

    Article Snippet: We also made polyclonal antibodies against the T. denticola membrane fraction with the same protocol through Alpha Diagnostics International, San Antonio, TX.

    Techniques: Cell Culture, Microscopy, Negative Control, Mutagenesis, Infection, Concentration Assay

    Analysis of fbp gene of T. denticola shows significant homology to other bacterial Fbp proteins in the FbpA family. A. Multiple alignment of FbpA proteins from T. denticola, T. vincentii, B. burgdorferi, S. pyogenes (Fbp54) and S. pneumoniae (PavA) by ClustalW. “*”; residues are identical in all sequences. “:”;conserved substitutions have been observed. “.”;semi-conserved substitutions are observed. B. Schematic diagram of identified domain structure of 471 residue Fbp protein. The FbpA domain is located in the N -terminal region with an internal deletion region. A domain of unknown function (DUF814) is located at C -terminal region.

    Journal: Anaerobe

    Article Title: Fibronectin-binding protein TDE1579 affects cytotoxicity of Treponema denticola

    doi: 10.1016/j.anaerobe.2015.09.010

    Figure Lengend Snippet: Analysis of fbp gene of T. denticola shows significant homology to other bacterial Fbp proteins in the FbpA family. A. Multiple alignment of FbpA proteins from T. denticola, T. vincentii, B. burgdorferi, S. pyogenes (Fbp54) and S. pneumoniae (PavA) by ClustalW. “*”; residues are identical in all sequences. “:”;conserved substitutions have been observed. “.”;semi-conserved substitutions are observed. B. Schematic diagram of identified domain structure of 471 residue Fbp protein. The FbpA domain is located in the N -terminal region with an internal deletion region. A domain of unknown function (DUF814) is located at C -terminal region.

    Article Snippet: We also made polyclonal antibodies against the T. denticola membrane fraction with the same protocol through Alpha Diagnostics International, San Antonio, TX.

    Techniques:

    A. Fbp was present in membrane and cytoplasmic fractions of wildtype T. denticola , but not in fbp mutant. B. T. denticola membrane treated at indicated temperature demonstrated that membrane proteins dissociated with heating. C. Fbp in T. denticola membrane was detected when T. denticola membrane was treated at temperature greater than 56 °C.

    Journal: Anaerobe

    Article Title: Fibronectin-binding protein TDE1579 affects cytotoxicity of Treponema denticola

    doi: 10.1016/j.anaerobe.2015.09.010

    Figure Lengend Snippet: A. Fbp was present in membrane and cytoplasmic fractions of wildtype T. denticola , but not in fbp mutant. B. T. denticola membrane treated at indicated temperature demonstrated that membrane proteins dissociated with heating. C. Fbp in T. denticola membrane was detected when T. denticola membrane was treated at temperature greater than 56 °C.

    Article Snippet: We also made polyclonal antibodies against the T. denticola membrane fraction with the same protocol through Alpha Diagnostics International, San Antonio, TX.

    Techniques: Mutagenesis

    Confirmation of T. denticola fbp deletion mutant by PCR. Wildtype strain and fbp mutant with various primer pairs showed that fbp gene in T. denticola mutant was replaced by erm cassette.

    Journal: Anaerobe

    Article Title: Fibronectin-binding protein TDE1579 affects cytotoxicity of Treponema denticola

    doi: 10.1016/j.anaerobe.2015.09.010

    Figure Lengend Snippet: Confirmation of T. denticola fbp deletion mutant by PCR. Wildtype strain and fbp mutant with various primer pairs showed that fbp gene in T. denticola mutant was replaced by erm cassette.

    Article Snippet: We also made polyclonal antibodies against the T. denticola membrane fraction with the same protocol through Alpha Diagnostics International, San Antonio, TX.

    Techniques: Mutagenesis, Polymerase Chain Reaction

    A. The binding of T. denticola to human FN and gingival fibroblast cells. No difference in bacterial FN binding between the wildtype strain and the fbp mutant was identified. Each value is the average and SD of three independent assays. B. The fbp mutant showed 51% reduced binding to hGF compared to wildtype. Each value is the average and SD of four independent assays.

    Journal: Anaerobe

    Article Title: Fibronectin-binding protein TDE1579 affects cytotoxicity of Treponema denticola

    doi: 10.1016/j.anaerobe.2015.09.010

    Figure Lengend Snippet: A. The binding of T. denticola to human FN and gingival fibroblast cells. No difference in bacterial FN binding between the wildtype strain and the fbp mutant was identified. Each value is the average and SD of three independent assays. B. The fbp mutant showed 51% reduced binding to hGF compared to wildtype. Each value is the average and SD of four independent assays.

    Article Snippet: We also made polyclonal antibodies against the T. denticola membrane fraction with the same protocol through Alpha Diagnostics International, San Antonio, TX.

    Techniques: Binding Assay, 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.

    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

    A phylogenetic split in spirochete mode of growth. ( A – D ) Cultures of spirochetes from different genera were incubated with variable concentrations of HADA for 30 min and analyzed at the single-cell level in a demograph. Heat map displays the relative fluorescence intensity in arbitrary units (0–1). ( A ) Borrelia miyamotoi strain LS-2000, 0.1 mM HADA, n = 173. ( B ) B. hermsii , 0.1 mM HADA, n = 391. ( C ) T. denticola ATCC 34505, 0.2 mM HADA, n = 2132. ( D ) L. interrogans serovar Conpenhageni strain Fiocruz L1-130, 0.4 mM HADA, n = 373. ( E ) Bar graphs depicting the percent of cells with a given number of zones.

    Journal: Proceedings of the National Academy of Sciences of the United States of America

    Article Title: Lyme disease and relapsing fever Borrelia elongate through zones of peptidoglycan synthesis that mark division sites of daughter cells

    doi: 10.1073/pnas.1610805113

    Figure Lengend Snippet: A phylogenetic split in spirochete mode of growth. ( A – D ) Cultures of spirochetes from different genera were incubated with variable concentrations of HADA for 30 min and analyzed at the single-cell level in a demograph. Heat map displays the relative fluorescence intensity in arbitrary units (0–1). ( A ) Borrelia miyamotoi strain LS-2000, 0.1 mM HADA, n = 173. ( B ) B. hermsii , 0.1 mM HADA, n = 391. ( C ) T. denticola ATCC 34505, 0.2 mM HADA, n = 2132. ( D ) L. interrogans serovar Conpenhageni strain Fiocruz L1-130, 0.4 mM HADA, n = 373. ( E ) Bar graphs depicting the percent of cells with a given number of zones.

    Article Snippet: T. denticola ATCC 34505 was propagated at 37 °C in supplemented TYGVS medium ( ) in an anaerobic chamber under an atmosphere mixture of N2 :H2 :CO2 (80:10:10).

    Techniques: Incubation, Fluorescence