t denticola strains  (ATCC)


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    Structured Review

    ATCC t denticola strains
    Effects of exposure time, dentilisin protease, and the major outer sheath protein on the susceptibility of T. <t>denticola</t> to LL-37. T. denticola TD4 and T. denticola mutants K1 (lacking the outer sheath protease dentilisin) and MHE (lacking the major outer sheath protein) were incubated with 50 μg/ml LL-37 for the indicated times and were analyzed for intracellular ATP levels. The data are means and standard deviations for three independent experiments performed in duplicate. *, P
    T Denticola Strains, supplied by ATCC, used in various techniques. Bioz Stars score: 93/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "The Antibacterial Activity of LL-37 against Treponema denticola Is Dentilisin Protease Independent and Facilitated by the Major Outer Sheath Protein Virulence Factor"

    Article Title: The Antibacterial Activity of LL-37 against Treponema denticola Is Dentilisin Protease Independent and Facilitated by the Major Outer Sheath Protein Virulence Factor

    Journal: Infection and Immunity

    doi: 10.1128/IAI.05903-11

    Effects of exposure time, dentilisin protease, and the major outer sheath protein on the susceptibility of T. denticola to LL-37. T. denticola TD4 and T. denticola mutants K1 (lacking the outer sheath protease dentilisin) and MHE (lacking the major outer sheath protein) were incubated with 50 μg/ml LL-37 for the indicated times and were analyzed for intracellular ATP levels. The data are means and standard deviations for three independent experiments performed in duplicate. *, P
    Figure Legend Snippet: Effects of exposure time, dentilisin protease, and the major outer sheath protein on the susceptibility of T. denticola to LL-37. T. denticola TD4 and T. denticola mutants K1 (lacking the outer sheath protease dentilisin) and MHE (lacking the major outer sheath protein) were incubated with 50 μg/ml LL-37 for the indicated times and were analyzed for intracellular ATP levels. The data are means and standard deviations for three independent experiments performed in duplicate. *, P

    Techniques Used: Incubation

    LL-37 degradation by the T. denticola dentilisin. (A) LL-37 (10 μg) was incubated for 2 h at 37°C without (a) or with T. denticola TD4 (wild-type) supernatant (b), T. denticola K1 (dentilisin activity-deficient) supernatant (c), or T. denticola TD4 supernatant preincubated (20 min) with either 1 mM PMSF (d), 0.4 mM chymostatin (e), or saliva (13 μl cleared saliva/10 μl supernatant) (f). (B) LL-37 was incubated as described above without (a) or with purified dentilisin in the absence (b) or presence (c) of saliva (13 μl cleared saliva/2 × 10 −3 U purified dentilisin).
    Figure Legend Snippet: LL-37 degradation by the T. denticola dentilisin. (A) LL-37 (10 μg) was incubated for 2 h at 37°C without (a) or with T. denticola TD4 (wild-type) supernatant (b), T. denticola K1 (dentilisin activity-deficient) supernatant (c), or T. denticola TD4 supernatant preincubated (20 min) with either 1 mM PMSF (d), 0.4 mM chymostatin (e), or saliva (13 μl cleared saliva/10 μl supernatant) (f). (B) LL-37 was incubated as described above without (a) or with purified dentilisin in the absence (b) or presence (c) of saliva (13 μl cleared saliva/2 × 10 −3 U purified dentilisin).

    Techniques Used: Incubation, Activity Assay, Purification

    The binding of Alexa Fluor 350-labeled LL-37 to T. denticola is enhanced by the major outer sheath protein. Wild-type TD4 (A) and MHE mutant (lacking the major outer sheath protein) (B) cells were incubated with Alexa Fluor 350-labeled LL-37 and were analyzed by flow cytometry. Light shaded histograms, unlabeled bacteria; dark shaded histograms, bacteria reacted with Alexa Fluor 350-labeled LL-37. The geometric mean number for each histogram is given. The results shown are representative of three separate experiments.
    Figure Legend Snippet: The binding of Alexa Fluor 350-labeled LL-37 to T. denticola is enhanced by the major outer sheath protein. Wild-type TD4 (A) and MHE mutant (lacking the major outer sheath protein) (B) cells were incubated with Alexa Fluor 350-labeled LL-37 and were analyzed by flow cytometry. Light shaded histograms, unlabeled bacteria; dark shaded histograms, bacteria reacted with Alexa Fluor 350-labeled LL-37. The geometric mean number for each histogram is given. The results shown are representative of three separate experiments.

    Techniques Used: Binding Assay, Labeling, Mutagenesis, Incubation, Flow Cytometry, Cytometry

    Inhibition of T. denticola growth by LL-37. T. denticola TD4 (ATCC 35404) (1 × 10 8 cells/ml) was inoculated in GM-1 medium under anaerobic conditions at 37°C with or without increasing concentrations of LL-37. Bacterial growth was measured spectrophotometrically at 660 nm after 4 days. The optical density at time zero was considered 100% growth inhibition. The optical density of bacterial growth in the absence of LL-37 was considered 0% growth inhibition. The data are means and standard deviations for a representative experiment performed in triplicate and repeated twice.
    Figure Legend Snippet: Inhibition of T. denticola growth by LL-37. T. denticola TD4 (ATCC 35404) (1 × 10 8 cells/ml) was inoculated in GM-1 medium under anaerobic conditions at 37°C with or without increasing concentrations of LL-37. Bacterial growth was measured spectrophotometrically at 660 nm after 4 days. The optical density at time zero was considered 100% growth inhibition. The optical density of bacterial growth in the absence of LL-37 was considered 0% growth inhibition. The data are means and standard deviations for a representative experiment performed in triplicate and repeated twice.

    Techniques Used: Inhibition

    Inactivation of LL-37 by T. denticola supernatant. LL-37 incubated for 2 h without or with T. denticola supernatant or with heat-inactivated supernatant (boiled) was added to a growing culture of T. denticola TD4 (50 μg/ml) (A) or E. coli (20 μg/ml) (B). (A) Intracellular ATP was measured to calculate the percentage of treponeme survival. ATP levels of bacteria not treated with LL-37 were considered to represent 100% survival, and ATP levels of heat-killed bacteria (exposure to 100°C for 5 min) were defined as 0% survival. Data are means and standard deviations for three independent experiments performed in duplicate. *, P
    Figure Legend Snippet: Inactivation of LL-37 by T. denticola supernatant. LL-37 incubated for 2 h without or with T. denticola supernatant or with heat-inactivated supernatant (boiled) was added to a growing culture of T. denticola TD4 (50 μg/ml) (A) or E. coli (20 μg/ml) (B). (A) Intracellular ATP was measured to calculate the percentage of treponeme survival. ATP levels of bacteria not treated with LL-37 were considered to represent 100% survival, and ATP levels of heat-killed bacteria (exposure to 100°C for 5 min) were defined as 0% survival. Data are means and standard deviations for three independent experiments performed in duplicate. *, P

    Techniques Used: Incubation

    Related Articles

    Concentration Assay:

    Article Title: The Antibacterial Activity of LL-37 against Treponema denticola Is Dentilisin Protease Independent and Facilitated by the Major Outer Sheath Protein Virulence Factor
    Article Snippet: As shown in , an LL-37 concentration of 50 μg/ml (11 μM) or higher inhibited the growth of T. denticola ATCC 35404 (TD4) by 85%. .. To determine whether susceptibility to LL-37 is common among T. denticola strains, growth inhibition by LL-37 (50 μg/ml) was also tested with T. denticola ATCC 33520 and GM-1.

    Inhibition:

    Article Title: The Antibacterial Activity of LL-37 against Treponema denticola Is Dentilisin Protease Independent and Facilitated by the Major Outer Sheath Protein Virulence Factor
    Article Snippet: .. To determine whether susceptibility to LL-37 is common among T. denticola strains, growth inhibition by LL-37 (50 μg/ml) was also tested with T. denticola ATCC 33520 and GM-1. ..

    Activity Assay:

    Article Title: The Antibacterial Activity of LL-37 against Treponema denticola Is Dentilisin Protease Independent and Facilitated by the Major Outer Sheath Protein Virulence Factor
    Article Snippet: Paragraph title: Antibacterial activity of LL-37 against T. denticola . ... To determine whether susceptibility to LL-37 is common among T. denticola strains, growth inhibition by LL-37 (50 μg/ml) was also tested with T. denticola ATCC 33520 and GM-1.

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    ATCC t denticola atcc 35405
    Construction of T. <t>denticola</t> mutants using ermF-ermB and ermB cassettes. The protease operon ( prcB-prcA-prtP ) and adjacent gene TDE0759 in wildtype parent strain <t>ATCC</t> 35405 and isogenic strains mutated in prcB (P0760 and CF548) and prcA (PNE and CF547) showing locations of ermF-ermB and ermB insertions. The symbol x- indicates gene disruption in prcA or prcB .
    T Denticola Atcc 35405, supplied by ATCC, used in various techniques. Bioz Stars score: 99/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    ATCC t denticola
    Histogram of fluorescence intensity of rhodamine-phalloidin-labeled F-actin in HGF during a 140-min time course, analyzed by confocal microscopy. There was significant depolymerization of F-actin in the T. <t>denticola</t> ATCC 35405-challenged HGF (left graph) in comparison with the control HGF (right graph). The degree of diminished fluorescence in T. denticola -challenged cells was significant at 60 min ( P
    T Denticola, supplied by ATCC, used in various techniques. Bioz Stars score: 93/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


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

    Journal: Journal of microbiological methods

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

    doi: 10.1016/j.mimet.2010.07.020

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

    Article Snippet: T. denticola ATCC 35405 (the Type strain, which has been passaged extensively in various laboratories) was electroporated with the resulting linear DNA s and plated in NOS-GN soft agar medium containing erythromycin (40 μg ml−1 , Sigma Chemical Co., St. Louis, MO) as described previously.

    Techniques:

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

    Journal: Infection and Immunity

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

    doi:

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

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

    Techniques: Fluorescence, Labeling, Confocal Microscopy

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

    Journal: Infection and Immunity

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

    doi:

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

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

    Techniques: Standard Deviation

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

    Journal: Infection and Immunity

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

    doi:

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

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

    Techniques: SDS Page, Nucleic Acid Electrophoresis

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

    Journal: Infection and Immunity

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

    doi: 10.1128/IAI.69.7.4465-4472.2001

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

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

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

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

    Journal: Infection and Immunity

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

    doi: 10.1128/IAI.69.7.4465-4472.2001

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

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

    Techniques:

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

    Journal: Infection and Immunity

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

    doi: 10.1128/IAI.69.7.4465-4472.2001

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

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

    Techniques: Clone Assay, Polymerase Chain Reaction

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

    Journal: Infection and Immunity

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

    doi: 10.1128/IAI.69.7.4465-4472.2001

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

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

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