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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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    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 20 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 137 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    ATCC t denticola atcc 35405
    Localization of T. <t>denticola</t> major surface protein and protease complex polypeptides. A surface localization immunofluorescence assay was performed with T. denticola <t>ATCC</t> 35405 with or without membrane permeabilization, using polyclonal antibodies raised
    T Denticola Atcc 35405, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 689 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    ATCC t denticola atcc 700768
    Localization of T. <t>denticola</t> major surface protein and protease complex polypeptides. A surface localization immunofluorescence assay was performed with T. denticola <t>ATCC</t> 35405 with or without membrane permeabilization, using polyclonal antibodies raised
    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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    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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    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


    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

    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

    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: DNA sequences of the prcB ORF in T. denticola strains ATCC 33520 and OTK were amplified from genomic DNA with primers CX402 and CX360.

    Techniques: Sequencing

    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

    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

    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

    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

    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

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

    Journal: Infection and Immunity

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

    doi: 10.1128/IAI.69.10.6276-6283.2001

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

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

    Techniques: Mutagenesis

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

    Journal: Infection and Immunity

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

    doi: 10.1128/IAI.69.10.6276-6283.2001

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

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

    Techniques:

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

    Journal: Infection and Immunity

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

    doi: 10.1128/IAI.69.10.6276-6283.2001

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

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

    Techniques: Chemotaxis Assay, Mutagenesis

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

    Journal: Molecular oral microbiology

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

    doi: 10.1111/j.2041-1014.2010.00584.x

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

    Article Snippet: Comparisons between the T. pallidum Nichols and T. denticola ATCC 35405 genomes have become possible because they have both been fully sequenced and annotated.

    Techniques: Immunofluorescence, Negative Control

    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

    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: All components of the dentilisin operon (prcB, prcA and prtP) were found in T. pedis TA4 and had amino acid identities of 48%, 56%, and 67%, respectively when aligned to the corresponding T. denticola ATCC 35405 proteins.

    Techniques:

    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