t denticola atcc 35405  (ATCC)


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    Structured Review

    ATCC t denticola atcc 35405
    TCT in the absence or presence of T. <t>denticola</t> ATCC 35405, MHE (Msp − ), or CKE (CTLP − ). Human plasma was incubated with T. denticola (1.2 × 10 9 cells/ml) suspended in PBS or with PBS alone (control) for 5 min before the addition
    T Denticola Atcc 35405, supplied by ATCC, used in various techniques. Bioz Stars score: 93/100, based on 11 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Images

    1) Product Images from "The Chymotrypsin-Like Protease Complex of Treponema denticola ATCC 35405 Mediates Fibrinogen Adherence and Degradation ▿"

    Article Title: The Chymotrypsin-Like Protease Complex of Treponema denticola ATCC 35405 Mediates Fibrinogen Adherence and Degradation ▿

    Journal: Infection and Immunity

    doi: 10.1128/IAI.00258-07

    TCT in the absence or presence of T. denticola ATCC 35405, MHE (Msp − ), or CKE (CTLP − ). Human plasma was incubated with T. denticola (1.2 × 10 9 cells/ml) suspended in PBS or with PBS alone (control) for 5 min before the addition
    Figure Legend Snippet: TCT in the absence or presence of T. denticola ATCC 35405, MHE (Msp − ), or CKE (CTLP − ). Human plasma was incubated with T. denticola (1.2 × 10 9 cells/ml) suspended in PBS or with PBS alone (control) for 5 min before the addition

    Techniques Used: Incubation

    Fibrinogen zymograms of outer membrane proteins from T. denticola ATCC 35405, MHE (Msp − ), and CKE (CTLP − ). Triton X-114 extracts were incubated for 5 min at 20°C (−) or 100°C (+) before being subjected to
    Figure Legend Snippet: Fibrinogen zymograms of outer membrane proteins from T. denticola ATCC 35405, MHE (Msp − ), and CKE (CTLP − ). Triton X-114 extracts were incubated for 5 min at 20°C (−) or 100°C (+) before being subjected to

    Techniques Used: Incubation

    Purification and enzymatic activity of major fibrinogen-binding protein from T. denticola ATCC 35405. Outer membrane proteins were extracted with 0.1% Triton X-114 solution and incubated with fibrinogen-linked Sepharose, and then tightly bound
    Figure Legend Snippet: Purification and enzymatic activity of major fibrinogen-binding protein from T. denticola ATCC 35405. Outer membrane proteins were extracted with 0.1% Triton X-114 solution and incubated with fibrinogen-linked Sepharose, and then tightly bound

    Techniques Used: Purification, Activity Assay, Binding Assay, Incubation

    Binding of fluid-phase or immobilized fibrinogen by T. denticola ATCC 35405 (⧫), MHE (Msp − ; ▴), or CKE (CTLP − ; ▪). (A and B) Treponema cells immobilized onto plastic wells in the absence (A) or presence (B) of 0.05
    Figure Legend Snippet: Binding of fluid-phase or immobilized fibrinogen by T. denticola ATCC 35405 (⧫), MHE (Msp − ; ▴), or CKE (CTLP − ; ▪). (A and B) Treponema cells immobilized onto plastic wells in the absence (A) or presence (B) of 0.05

    Techniques Used: Binding Assay

    Fibrinogen blot overlay of outer membrane protein extracts from T. denticola ATCC 35405, MHE, and CKE. Proteins were extracted with 1% Triton X-114 and incubated for 5 min at 20°C (−) or 100°C (+) before being subjected
    Figure Legend Snippet: Fibrinogen blot overlay of outer membrane protein extracts from T. denticola ATCC 35405, MHE, and CKE. Proteins were extracted with 1% Triton X-114 and incubated for 5 min at 20°C (−) or 100°C (+) before being subjected

    Techniques Used: Incubation

    Adherence of T. denticola ATCC 35405 cells to denatured fibrinogen or recombinant fibrinogen polypeptides. (A) Human fibrinogen (N) or purified recombinant Aα, Bβ, and γ chain polypeptides were heated for 5 min at 100°C
    Figure Legend Snippet: Adherence of T. denticola ATCC 35405 cells to denatured fibrinogen or recombinant fibrinogen polypeptides. (A) Human fibrinogen (N) or purified recombinant Aα, Bβ, and γ chain polypeptides were heated for 5 min at 100°C

    Techniques Used: Recombinant, Purification

    2) Product Images from "The Chymotrypsin-Like Protease Complex of Treponema denticola ATCC 35405 Mediates Fibrinogen Adherence and Degradation ▿"

    Article Title: The Chymotrypsin-Like Protease Complex of Treponema denticola ATCC 35405 Mediates Fibrinogen Adherence and Degradation ▿

    Journal: Infection and Immunity

    doi: 10.1128/IAI.00258-07

    TCT in the absence or presence of T. denticola ATCC 35405, MHE (Msp − ), or CKE (CTLP − ). Human plasma was incubated with T. denticola (1.2 × 10 9 cells/ml) suspended in PBS or with PBS alone (control) for 5 min before the addition
    Figure Legend Snippet: TCT in the absence or presence of T. denticola ATCC 35405, MHE (Msp − ), or CKE (CTLP − ). Human plasma was incubated with T. denticola (1.2 × 10 9 cells/ml) suspended in PBS or with PBS alone (control) for 5 min before the addition

    Techniques Used: Incubation

    Fibrinogen zymograms of outer membrane proteins from T. denticola ATCC 35405, MHE (Msp − ), and CKE (CTLP − ). Triton X-114 extracts were incubated for 5 min at 20°C (−) or 100°C (+) before being subjected to
    Figure Legend Snippet: Fibrinogen zymograms of outer membrane proteins from T. denticola ATCC 35405, MHE (Msp − ), and CKE (CTLP − ). Triton X-114 extracts were incubated for 5 min at 20°C (−) or 100°C (+) before being subjected to

    Techniques Used: Incubation

    Purification and enzymatic activity of major fibrinogen-binding protein from T. denticola ATCC 35405. Outer membrane proteins were extracted with 0.1% Triton X-114 solution and incubated with fibrinogen-linked Sepharose, and then tightly bound
    Figure Legend Snippet: Purification and enzymatic activity of major fibrinogen-binding protein from T. denticola ATCC 35405. Outer membrane proteins were extracted with 0.1% Triton X-114 solution and incubated with fibrinogen-linked Sepharose, and then tightly bound

    Techniques Used: Purification, Activity Assay, Binding Assay, Incubation

    Binding of fluid-phase or immobilized fibrinogen by T. denticola ATCC 35405 (⧫), MHE (Msp − ; ▴), or CKE (CTLP − ; ▪). (A and B) Treponema cells immobilized onto plastic wells in the absence (A) or presence (B) of 0.05
    Figure Legend Snippet: Binding of fluid-phase or immobilized fibrinogen by T. denticola ATCC 35405 (⧫), MHE (Msp − ; ▴), or CKE (CTLP − ; ▪). (A and B) Treponema cells immobilized onto plastic wells in the absence (A) or presence (B) of 0.05

    Techniques Used: Binding Assay

    Fibrinogen blot overlay of outer membrane protein extracts from T. denticola ATCC 35405, MHE, and CKE. Proteins were extracted with 1% Triton X-114 and incubated for 5 min at 20°C (−) or 100°C (+) before being subjected
    Figure Legend Snippet: Fibrinogen blot overlay of outer membrane protein extracts from T. denticola ATCC 35405, MHE, and CKE. Proteins were extracted with 1% Triton X-114 and incubated for 5 min at 20°C (−) or 100°C (+) before being subjected

    Techniques Used: Incubation

    Adherence of T. denticola ATCC 35405 cells to denatured fibrinogen or recombinant fibrinogen polypeptides. (A) Human fibrinogen (N) or purified recombinant Aα, Bβ, and γ chain polypeptides were heated for 5 min at 100°C
    Figure Legend Snippet: Adherence of T. denticola ATCC 35405 cells to denatured fibrinogen or recombinant fibrinogen polypeptides. (A) Human fibrinogen (N) or purified recombinant Aα, Bβ, and γ chain polypeptides were heated for 5 min at 100°C

    Techniques Used: Recombinant, Purification

    3) Product Images from "The Chymotrypsin-Like Protease Complex of Treponema denticola ATCC 35405 Mediates Fibrinogen Adherence and Degradation ▿"

    Article Title: The Chymotrypsin-Like Protease Complex of Treponema denticola ATCC 35405 Mediates Fibrinogen Adherence and Degradation ▿

    Journal: Infection and Immunity

    doi: 10.1128/IAI.00258-07

    TCT in the absence or presence of T. denticola ATCC 35405, MHE (Msp − ), or CKE (CTLP − ). Human plasma was incubated with T. denticola (1.2 × 10 9 cells/ml) suspended in PBS or with PBS alone (control) for 5 min before the addition
    Figure Legend Snippet: TCT in the absence or presence of T. denticola ATCC 35405, MHE (Msp − ), or CKE (CTLP − ). Human plasma was incubated with T. denticola (1.2 × 10 9 cells/ml) suspended in PBS or with PBS alone (control) for 5 min before the addition

    Techniques Used: Incubation

    Fibrinogen zymograms of outer membrane proteins from T. denticola ATCC 35405, MHE (Msp − ), and CKE (CTLP − ). Triton X-114 extracts were incubated for 5 min at 20°C (−) or 100°C (+) before being subjected to
    Figure Legend Snippet: Fibrinogen zymograms of outer membrane proteins from T. denticola ATCC 35405, MHE (Msp − ), and CKE (CTLP − ). Triton X-114 extracts were incubated for 5 min at 20°C (−) or 100°C (+) before being subjected to

    Techniques Used: Incubation

    Purification and enzymatic activity of major fibrinogen-binding protein from T. denticola ATCC 35405. Outer membrane proteins were extracted with 0.1% Triton X-114 solution and incubated with fibrinogen-linked Sepharose, and then tightly bound
    Figure Legend Snippet: Purification and enzymatic activity of major fibrinogen-binding protein from T. denticola ATCC 35405. Outer membrane proteins were extracted with 0.1% Triton X-114 solution and incubated with fibrinogen-linked Sepharose, and then tightly bound

    Techniques Used: Purification, Activity Assay, Binding Assay, Incubation

    Binding of fluid-phase or immobilized fibrinogen by T. denticola ATCC 35405 (⧫), MHE (Msp − ; ▴), or CKE (CTLP − ; ▪). (A and B) Treponema cells immobilized onto plastic wells in the absence (A) or presence (B) of 0.05
    Figure Legend Snippet: Binding of fluid-phase or immobilized fibrinogen by T. denticola ATCC 35405 (⧫), MHE (Msp − ; ▴), or CKE (CTLP − ; ▪). (A and B) Treponema cells immobilized onto plastic wells in the absence (A) or presence (B) of 0.05

    Techniques Used: Binding Assay

    Fibrinogen blot overlay of outer membrane protein extracts from T. denticola ATCC 35405, MHE, and CKE. Proteins were extracted with 1% Triton X-114 and incubated for 5 min at 20°C (−) or 100°C (+) before being subjected
    Figure Legend Snippet: Fibrinogen blot overlay of outer membrane protein extracts from T. denticola ATCC 35405, MHE, and CKE. Proteins were extracted with 1% Triton X-114 and incubated for 5 min at 20°C (−) or 100°C (+) before being subjected

    Techniques Used: Incubation

    Adherence of T. denticola ATCC 35405 cells to denatured fibrinogen or recombinant fibrinogen polypeptides. (A) Human fibrinogen (N) or purified recombinant Aα, Bβ, and γ chain polypeptides were heated for 5 min at 100°C
    Figure Legend Snippet: Adherence of T. denticola ATCC 35405 cells to denatured fibrinogen or recombinant fibrinogen polypeptides. (A) Human fibrinogen (N) or purified recombinant Aα, Bβ, and γ chain polypeptides were heated for 5 min at 100°C

    Techniques Used: Recombinant, Purification

    4) Product Images from "The Chymotrypsin-Like Protease Complex of Treponema denticola ATCC 35405 Mediates Fibrinogen Adherence and Degradation ▿"

    Article Title: The Chymotrypsin-Like Protease Complex of Treponema denticola ATCC 35405 Mediates Fibrinogen Adherence and Degradation ▿

    Journal: Infection and Immunity

    doi: 10.1128/IAI.00258-07

    TCT in the absence or presence of T. denticola ATCC 35405, MHE (Msp − ), or CKE (CTLP − ). Human plasma was incubated with T. denticola (1.2 × 10 9 cells/ml) suspended in PBS or with PBS alone (control) for 5 min before the addition
    Figure Legend Snippet: TCT in the absence or presence of T. denticola ATCC 35405, MHE (Msp − ), or CKE (CTLP − ). Human plasma was incubated with T. denticola (1.2 × 10 9 cells/ml) suspended in PBS or with PBS alone (control) for 5 min before the addition

    Techniques Used: Incubation

    Fibrinogen zymograms of outer membrane proteins from T. denticola ATCC 35405, MHE (Msp − ), and CKE (CTLP − ). Triton X-114 extracts were incubated for 5 min at 20°C (−) or 100°C (+) before being subjected to
    Figure Legend Snippet: Fibrinogen zymograms of outer membrane proteins from T. denticola ATCC 35405, MHE (Msp − ), and CKE (CTLP − ). Triton X-114 extracts were incubated for 5 min at 20°C (−) or 100°C (+) before being subjected to

    Techniques Used: Incubation

    Purification and enzymatic activity of major fibrinogen-binding protein from T. denticola ATCC 35405. Outer membrane proteins were extracted with 0.1% Triton X-114 solution and incubated with fibrinogen-linked Sepharose, and then tightly bound
    Figure Legend Snippet: Purification and enzymatic activity of major fibrinogen-binding protein from T. denticola ATCC 35405. Outer membrane proteins were extracted with 0.1% Triton X-114 solution and incubated with fibrinogen-linked Sepharose, and then tightly bound

    Techniques Used: Purification, Activity Assay, Binding Assay, Incubation

    Binding of fluid-phase or immobilized fibrinogen by T. denticola ATCC 35405 (⧫), MHE (Msp − ; ▴), or CKE (CTLP − ; ▪). (A and B) Treponema cells immobilized onto plastic wells in the absence (A) or presence (B) of 0.05
    Figure Legend Snippet: Binding of fluid-phase or immobilized fibrinogen by T. denticola ATCC 35405 (⧫), MHE (Msp − ; ▴), or CKE (CTLP − ; ▪). (A and B) Treponema cells immobilized onto plastic wells in the absence (A) or presence (B) of 0.05

    Techniques Used: Binding Assay

    Fibrinogen blot overlay of outer membrane protein extracts from T. denticola ATCC 35405, MHE, and CKE. Proteins were extracted with 1% Triton X-114 and incubated for 5 min at 20°C (−) or 100°C (+) before being subjected
    Figure Legend Snippet: Fibrinogen blot overlay of outer membrane protein extracts from T. denticola ATCC 35405, MHE, and CKE. Proteins were extracted with 1% Triton X-114 and incubated for 5 min at 20°C (−) or 100°C (+) before being subjected

    Techniques Used: Incubation

    Adherence of T. denticola ATCC 35405 cells to denatured fibrinogen or recombinant fibrinogen polypeptides. (A) Human fibrinogen (N) or purified recombinant Aα, Bβ, and γ chain polypeptides were heated for 5 min at 100°C
    Figure Legend Snippet: Adherence of T. denticola ATCC 35405 cells to denatured fibrinogen or recombinant fibrinogen polypeptides. (A) Human fibrinogen (N) or purified recombinant Aα, Bβ, and γ chain polypeptides were heated for 5 min at 100°C

    Techniques Used: Recombinant, Purification

    5) Product Images from "The Chymotrypsin-Like Protease Complex of Treponema denticola ATCC 35405 Mediates Fibrinogen Adherence and Degradation ▿"

    Article Title: The Chymotrypsin-Like Protease Complex of Treponema denticola ATCC 35405 Mediates Fibrinogen Adherence and Degradation ▿

    Journal: Infection and Immunity

    doi: 10.1128/IAI.00258-07

    TCT in the absence or presence of T. denticola ATCC 35405, MHE (Msp − ), or CKE (CTLP − ). Human plasma was incubated with T. denticola (1.2 × 10 9 cells/ml) suspended in PBS or with PBS alone (control) for 5 min before the addition
    Figure Legend Snippet: TCT in the absence or presence of T. denticola ATCC 35405, MHE (Msp − ), or CKE (CTLP − ). Human plasma was incubated with T. denticola (1.2 × 10 9 cells/ml) suspended in PBS or with PBS alone (control) for 5 min before the addition

    Techniques Used: Incubation

    Fibrinogen zymograms of outer membrane proteins from T. denticola ATCC 35405, MHE (Msp − ), and CKE (CTLP − ). Triton X-114 extracts were incubated for 5 min at 20°C (−) or 100°C (+) before being subjected to
    Figure Legend Snippet: Fibrinogen zymograms of outer membrane proteins from T. denticola ATCC 35405, MHE (Msp − ), and CKE (CTLP − ). Triton X-114 extracts were incubated for 5 min at 20°C (−) or 100°C (+) before being subjected to

    Techniques Used: Incubation

    Purification and enzymatic activity of major fibrinogen-binding protein from T. denticola ATCC 35405. Outer membrane proteins were extracted with 0.1% Triton X-114 solution and incubated with fibrinogen-linked Sepharose, and then tightly bound
    Figure Legend Snippet: Purification and enzymatic activity of major fibrinogen-binding protein from T. denticola ATCC 35405. Outer membrane proteins were extracted with 0.1% Triton X-114 solution and incubated with fibrinogen-linked Sepharose, and then tightly bound

    Techniques Used: Purification, Activity Assay, Binding Assay, Incubation

    Binding of fluid-phase or immobilized fibrinogen by T. denticola ATCC 35405 (⧫), MHE (Msp − ; ▴), or CKE (CTLP − ; ▪). (A and B) Treponema cells immobilized onto plastic wells in the absence (A) or presence (B) of 0.05
    Figure Legend Snippet: Binding of fluid-phase or immobilized fibrinogen by T. denticola ATCC 35405 (⧫), MHE (Msp − ; ▴), or CKE (CTLP − ; ▪). (A and B) Treponema cells immobilized onto plastic wells in the absence (A) or presence (B) of 0.05

    Techniques Used: Binding Assay

    Fibrinogen blot overlay of outer membrane protein extracts from T. denticola ATCC 35405, MHE, and CKE. Proteins were extracted with 1% Triton X-114 and incubated for 5 min at 20°C (−) or 100°C (+) before being subjected
    Figure Legend Snippet: Fibrinogen blot overlay of outer membrane protein extracts from T. denticola ATCC 35405, MHE, and CKE. Proteins were extracted with 1% Triton X-114 and incubated for 5 min at 20°C (−) or 100°C (+) before being subjected

    Techniques Used: Incubation

    Adherence of T. denticola ATCC 35405 cells to denatured fibrinogen or recombinant fibrinogen polypeptides. (A) Human fibrinogen (N) or purified recombinant Aα, Bβ, and γ chain polypeptides were heated for 5 min at 100°C
    Figure Legend Snippet: Adherence of T. denticola ATCC 35405 cells to denatured fibrinogen or recombinant fibrinogen polypeptides. (A) Human fibrinogen (N) or purified recombinant Aα, Bβ, and γ chain polypeptides were heated for 5 min at 100°C

    Techniques Used: Recombinant, Purification

    6) Product Images from "The Chymotrypsin-Like Protease Complex of Treponema denticola ATCC 35405 Mediates Fibrinogen Adherence and Degradation ▿"

    Article Title: The Chymotrypsin-Like Protease Complex of Treponema denticola ATCC 35405 Mediates Fibrinogen Adherence and Degradation ▿

    Journal: Infection and Immunity

    doi: 10.1128/IAI.00258-07

    TCT in the absence or presence of T. denticola ATCC 35405, MHE (Msp − ), or CKE (CTLP − ). Human plasma was incubated with T. denticola (1.2 × 10 9 cells/ml) suspended in PBS or with PBS alone (control) for 5 min before the addition
    Figure Legend Snippet: TCT in the absence or presence of T. denticola ATCC 35405, MHE (Msp − ), or CKE (CTLP − ). Human plasma was incubated with T. denticola (1.2 × 10 9 cells/ml) suspended in PBS or with PBS alone (control) for 5 min before the addition

    Techniques Used: Incubation

    Fibrinogen zymograms of outer membrane proteins from T. denticola ATCC 35405, MHE (Msp − ), and CKE (CTLP − ). Triton X-114 extracts were incubated for 5 min at 20°C (−) or 100°C (+) before being subjected to
    Figure Legend Snippet: Fibrinogen zymograms of outer membrane proteins from T. denticola ATCC 35405, MHE (Msp − ), and CKE (CTLP − ). Triton X-114 extracts were incubated for 5 min at 20°C (−) or 100°C (+) before being subjected to

    Techniques Used: Incubation

    Purification and enzymatic activity of major fibrinogen-binding protein from T. denticola ATCC 35405. Outer membrane proteins were extracted with 0.1% Triton X-114 solution and incubated with fibrinogen-linked Sepharose, and then tightly bound
    Figure Legend Snippet: Purification and enzymatic activity of major fibrinogen-binding protein from T. denticola ATCC 35405. Outer membrane proteins were extracted with 0.1% Triton X-114 solution and incubated with fibrinogen-linked Sepharose, and then tightly bound

    Techniques Used: Purification, Activity Assay, Binding Assay, Incubation

    Binding of fluid-phase or immobilized fibrinogen by T. denticola ATCC 35405 (⧫), MHE (Msp − ; ▴), or CKE (CTLP − ; ▪). (A and B) Treponema cells immobilized onto plastic wells in the absence (A) or presence (B) of 0.05
    Figure Legend Snippet: Binding of fluid-phase or immobilized fibrinogen by T. denticola ATCC 35405 (⧫), MHE (Msp − ; ▴), or CKE (CTLP − ; ▪). (A and B) Treponema cells immobilized onto plastic wells in the absence (A) or presence (B) of 0.05

    Techniques Used: Binding Assay

    Fibrinogen blot overlay of outer membrane protein extracts from T. denticola ATCC 35405, MHE, and CKE. Proteins were extracted with 1% Triton X-114 and incubated for 5 min at 20°C (−) or 100°C (+) before being subjected
    Figure Legend Snippet: Fibrinogen blot overlay of outer membrane protein extracts from T. denticola ATCC 35405, MHE, and CKE. Proteins were extracted with 1% Triton X-114 and incubated for 5 min at 20°C (−) or 100°C (+) before being subjected

    Techniques Used: Incubation

    Adherence of T. denticola ATCC 35405 cells to denatured fibrinogen or recombinant fibrinogen polypeptides. (A) Human fibrinogen (N) or purified recombinant Aα, Bβ, and γ chain polypeptides were heated for 5 min at 100°C
    Figure Legend Snippet: Adherence of T. denticola ATCC 35405 cells to denatured fibrinogen or recombinant fibrinogen polypeptides. (A) Human fibrinogen (N) or purified recombinant Aα, Bβ, and γ chain polypeptides were heated for 5 min at 100°C

    Techniques Used: Recombinant, Purification

    7) Product Images from "The Chymotrypsin-Like Protease Complex of Treponema denticola ATCC 35405 Mediates Fibrinogen Adherence and Degradation ▿"

    Article Title: The Chymotrypsin-Like Protease Complex of Treponema denticola ATCC 35405 Mediates Fibrinogen Adherence and Degradation ▿

    Journal: Infection and Immunity

    doi: 10.1128/IAI.00258-07

    TCT in the absence or presence of T. denticola ATCC 35405, MHE (Msp − ), or CKE (CTLP − ). Human plasma was incubated with T. denticola (1.2 × 10 9 cells/ml) suspended in PBS or with PBS alone (control) for 5 min before the addition
    Figure Legend Snippet: TCT in the absence or presence of T. denticola ATCC 35405, MHE (Msp − ), or CKE (CTLP − ). Human plasma was incubated with T. denticola (1.2 × 10 9 cells/ml) suspended in PBS or with PBS alone (control) for 5 min before the addition

    Techniques Used: Incubation

    Fibrinogen zymograms of outer membrane proteins from T. denticola ATCC 35405, MHE (Msp − ), and CKE (CTLP − ). Triton X-114 extracts were incubated for 5 min at 20°C (−) or 100°C (+) before being subjected to
    Figure Legend Snippet: Fibrinogen zymograms of outer membrane proteins from T. denticola ATCC 35405, MHE (Msp − ), and CKE (CTLP − ). Triton X-114 extracts were incubated for 5 min at 20°C (−) or 100°C (+) before being subjected to

    Techniques Used: Incubation

    Purification and enzymatic activity of major fibrinogen-binding protein from T. denticola ATCC 35405. Outer membrane proteins were extracted with 0.1% Triton X-114 solution and incubated with fibrinogen-linked Sepharose, and then tightly bound
    Figure Legend Snippet: Purification and enzymatic activity of major fibrinogen-binding protein from T. denticola ATCC 35405. Outer membrane proteins were extracted with 0.1% Triton X-114 solution and incubated with fibrinogen-linked Sepharose, and then tightly bound

    Techniques Used: Purification, Activity Assay, Binding Assay, Incubation

    Binding of fluid-phase or immobilized fibrinogen by T. denticola ATCC 35405 (⧫), MHE (Msp − ; ▴), or CKE (CTLP − ; ▪). (A and B) Treponema cells immobilized onto plastic wells in the absence (A) or presence (B) of 0.05
    Figure Legend Snippet: Binding of fluid-phase or immobilized fibrinogen by T. denticola ATCC 35405 (⧫), MHE (Msp − ; ▴), or CKE (CTLP − ; ▪). (A and B) Treponema cells immobilized onto plastic wells in the absence (A) or presence (B) of 0.05

    Techniques Used: Binding Assay

    Fibrinogen blot overlay of outer membrane protein extracts from T. denticola ATCC 35405, MHE, and CKE. Proteins were extracted with 1% Triton X-114 and incubated for 5 min at 20°C (−) or 100°C (+) before being subjected
    Figure Legend Snippet: Fibrinogen blot overlay of outer membrane protein extracts from T. denticola ATCC 35405, MHE, and CKE. Proteins were extracted with 1% Triton X-114 and incubated for 5 min at 20°C (−) or 100°C (+) before being subjected

    Techniques Used: Incubation

    Adherence of T. denticola ATCC 35405 cells to denatured fibrinogen or recombinant fibrinogen polypeptides. (A) Human fibrinogen (N) or purified recombinant Aα, Bβ, and γ chain polypeptides were heated for 5 min at 100°C
    Figure Legend Snippet: Adherence of T. denticola ATCC 35405 cells to denatured fibrinogen or recombinant fibrinogen polypeptides. (A) Human fibrinogen (N) or purified recombinant Aα, Bβ, and γ chain polypeptides were heated for 5 min at 100°C

    Techniques Used: Recombinant, Purification

    8) Product Images from "The Chymotrypsin-Like Protease Complex of Treponema denticola ATCC 35405 Mediates Fibrinogen Adherence and Degradation ▿"

    Article Title: The Chymotrypsin-Like Protease Complex of Treponema denticola ATCC 35405 Mediates Fibrinogen Adherence and Degradation ▿

    Journal: Infection and Immunity

    doi: 10.1128/IAI.00258-07

    TCT in the absence or presence of T. denticola ATCC 35405, MHE (Msp − ), or CKE (CTLP − ). Human plasma was incubated with T. denticola (1.2 × 10 9 cells/ml) suspended in PBS or with PBS alone (control) for 5 min before the addition
    Figure Legend Snippet: TCT in the absence or presence of T. denticola ATCC 35405, MHE (Msp − ), or CKE (CTLP − ). Human plasma was incubated with T. denticola (1.2 × 10 9 cells/ml) suspended in PBS or with PBS alone (control) for 5 min before the addition

    Techniques Used: Incubation

    Fibrinogen zymograms of outer membrane proteins from T. denticola ATCC 35405, MHE (Msp − ), and CKE (CTLP − ). Triton X-114 extracts were incubated for 5 min at 20°C (−) or 100°C (+) before being subjected to
    Figure Legend Snippet: Fibrinogen zymograms of outer membrane proteins from T. denticola ATCC 35405, MHE (Msp − ), and CKE (CTLP − ). Triton X-114 extracts were incubated for 5 min at 20°C (−) or 100°C (+) before being subjected to

    Techniques Used: Incubation

    Purification and enzymatic activity of major fibrinogen-binding protein from T. denticola ATCC 35405. Outer membrane proteins were extracted with 0.1% Triton X-114 solution and incubated with fibrinogen-linked Sepharose, and then tightly bound
    Figure Legend Snippet: Purification and enzymatic activity of major fibrinogen-binding protein from T. denticola ATCC 35405. Outer membrane proteins were extracted with 0.1% Triton X-114 solution and incubated with fibrinogen-linked Sepharose, and then tightly bound

    Techniques Used: Purification, Activity Assay, Binding Assay, Incubation

    Binding of fluid-phase or immobilized fibrinogen by T. denticola ATCC 35405 (⧫), MHE (Msp − ; ▴), or CKE (CTLP − ; ▪). (A and B) Treponema cells immobilized onto plastic wells in the absence (A) or presence (B) of 0.05
    Figure Legend Snippet: Binding of fluid-phase or immobilized fibrinogen by T. denticola ATCC 35405 (⧫), MHE (Msp − ; ▴), or CKE (CTLP − ; ▪). (A and B) Treponema cells immobilized onto plastic wells in the absence (A) or presence (B) of 0.05

    Techniques Used: Binding Assay

    Fibrinogen blot overlay of outer membrane protein extracts from T. denticola ATCC 35405, MHE, and CKE. Proteins were extracted with 1% Triton X-114 and incubated for 5 min at 20°C (−) or 100°C (+) before being subjected
    Figure Legend Snippet: Fibrinogen blot overlay of outer membrane protein extracts from T. denticola ATCC 35405, MHE, and CKE. Proteins were extracted with 1% Triton X-114 and incubated for 5 min at 20°C (−) or 100°C (+) before being subjected

    Techniques Used: Incubation

    Adherence of T. denticola ATCC 35405 cells to denatured fibrinogen or recombinant fibrinogen polypeptides. (A) Human fibrinogen (N) or purified recombinant Aα, Bβ, and γ chain polypeptides were heated for 5 min at 100°C
    Figure Legend Snippet: Adherence of T. denticola ATCC 35405 cells to denatured fibrinogen or recombinant fibrinogen polypeptides. (A) Human fibrinogen (N) or purified recombinant Aα, Bβ, and γ chain polypeptides were heated for 5 min at 100°C

    Techniques Used: Recombinant, Purification

    9) Product Images from "The Chymotrypsin-Like Protease Complex of Treponema denticola ATCC 35405 Mediates Fibrinogen Adherence and Degradation ▿"

    Article Title: The Chymotrypsin-Like Protease Complex of Treponema denticola ATCC 35405 Mediates Fibrinogen Adherence and Degradation ▿

    Journal: Infection and Immunity

    doi: 10.1128/IAI.00258-07

    TCT in the absence or presence of T. denticola ATCC 35405, MHE (Msp − ), or CKE (CTLP − ). Human plasma was incubated with T. denticola (1.2 × 10 9 cells/ml) suspended in PBS or with PBS alone (control) for 5 min before the addition
    Figure Legend Snippet: TCT in the absence or presence of T. denticola ATCC 35405, MHE (Msp − ), or CKE (CTLP − ). Human plasma was incubated with T. denticola (1.2 × 10 9 cells/ml) suspended in PBS or with PBS alone (control) for 5 min before the addition

    Techniques Used: Incubation

    Fibrinogen zymograms of outer membrane proteins from T. denticola ATCC 35405, MHE (Msp − ), and CKE (CTLP − ). Triton X-114 extracts were incubated for 5 min at 20°C (−) or 100°C (+) before being subjected to
    Figure Legend Snippet: Fibrinogen zymograms of outer membrane proteins from T. denticola ATCC 35405, MHE (Msp − ), and CKE (CTLP − ). Triton X-114 extracts were incubated for 5 min at 20°C (−) or 100°C (+) before being subjected to

    Techniques Used: Incubation

    Purification and enzymatic activity of major fibrinogen-binding protein from T. denticola ATCC 35405. Outer membrane proteins were extracted with 0.1% Triton X-114 solution and incubated with fibrinogen-linked Sepharose, and then tightly bound
    Figure Legend Snippet: Purification and enzymatic activity of major fibrinogen-binding protein from T. denticola ATCC 35405. Outer membrane proteins were extracted with 0.1% Triton X-114 solution and incubated with fibrinogen-linked Sepharose, and then tightly bound

    Techniques Used: Purification, Activity Assay, Binding Assay, Incubation

    Binding of fluid-phase or immobilized fibrinogen by T. denticola ATCC 35405 (⧫), MHE (Msp − ; ▴), or CKE (CTLP − ; ▪). (A and B) Treponema cells immobilized onto plastic wells in the absence (A) or presence (B) of 0.05
    Figure Legend Snippet: Binding of fluid-phase or immobilized fibrinogen by T. denticola ATCC 35405 (⧫), MHE (Msp − ; ▴), or CKE (CTLP − ; ▪). (A and B) Treponema cells immobilized onto plastic wells in the absence (A) or presence (B) of 0.05

    Techniques Used: Binding Assay

    Fibrinogen blot overlay of outer membrane protein extracts from T. denticola ATCC 35405, MHE, and CKE. Proteins were extracted with 1% Triton X-114 and incubated for 5 min at 20°C (−) or 100°C (+) before being subjected
    Figure Legend Snippet: Fibrinogen blot overlay of outer membrane protein extracts from T. denticola ATCC 35405, MHE, and CKE. Proteins were extracted with 1% Triton X-114 and incubated for 5 min at 20°C (−) or 100°C (+) before being subjected

    Techniques Used: Incubation

    Adherence of T. denticola ATCC 35405 cells to denatured fibrinogen or recombinant fibrinogen polypeptides. (A) Human fibrinogen (N) or purified recombinant Aα, Bβ, and γ chain polypeptides were heated for 5 min at 100°C
    Figure Legend Snippet: Adherence of T. denticola ATCC 35405 cells to denatured fibrinogen or recombinant fibrinogen polypeptides. (A) Human fibrinogen (N) or purified recombinant Aα, Bβ, and γ chain polypeptides were heated for 5 min at 100°C

    Techniques Used: Recombinant, Purification

    10) Product Images from "Binding Properties and Adhesion-Mediating Regions of the Major Sheath Protein of Treponema denticola ATCC 35405"

    Article Title: Binding Properties and Adhesion-Mediating Regions of the Major Sheath Protein of Treponema denticola ATCC 35405

    Journal: Infection and Immunity

    doi: 10.1128/IAI.73.5.2891-2898.2005

    Interactions of rMsp antibodies with T. denticola ATCC 35405 cells and of whole-cell antibodies with rMsp fragments. (Panel A) Reactivity in ELISA of antiserum (1:250 diluted) to T. denticola ATCC 35405 cells (W) or antisera (1:250 diluted) raised to
    Figure Legend Snippet: Interactions of rMsp antibodies with T. denticola ATCC 35405 cells and of whole-cell antibodies with rMsp fragments. (Panel A) Reactivity in ELISA of antiserum (1:250 diluted) to T. denticola ATCC 35405 cells (W) or antisera (1:250 diluted) raised to

    Techniques Used: Enzyme-linked Immunosorbent Assay

    Reactivities of Msp antisera with T. denticola ATCC 35405 outer membrane protein extracts. (Panel A) SDS-PAGE gel of outer membrane proteins. (Panel B) Western blots reacted with antisera to rN-Msp (lane 1), rV-Msp (lane 2), or rC-Msp (lane 3). Molecular
    Figure Legend Snippet: Reactivities of Msp antisera with T. denticola ATCC 35405 outer membrane protein extracts. (Panel A) SDS-PAGE gel of outer membrane proteins. (Panel B) Western blots reacted with antisera to rN-Msp (lane 1), rV-Msp (lane 2), or rC-Msp (lane 3). Molecular

    Techniques Used: SDS Page, Western Blot

    Binding of rMsp to human fibronectin and to 30-kDa N-terminal fragment of human fibronectin. (Panel A) Western blot overlay of trypsin-derived fragments of human plasma fibronectin reacted with rMsp (lane 1) or with biotinylated T. denticola ATCC 35405
    Figure Legend Snippet: Binding of rMsp to human fibronectin and to 30-kDa N-terminal fragment of human fibronectin. (Panel A) Western blot overlay of trypsin-derived fragments of human plasma fibronectin reacted with rMsp (lane 1) or with biotinylated T. denticola ATCC 35405

    Techniques Used: Binding Assay, Western Blot, Derivative Assay

    Diagrammatic representation of the Msp sequences from T. denticola ATCC 35520 (A), strain ATCC 35405 (B), and of recombinant Msp polypeptides rMsp (530 aa residues), rN-Msp (189 aa residues), rV-Msp (57 aa residues), and rN-Msp (272 aa residues), with
    Figure Legend Snippet: Diagrammatic representation of the Msp sequences from T. denticola ATCC 35520 (A), strain ATCC 35405 (B), and of recombinant Msp polypeptides rMsp (530 aa residues), rN-Msp (189 aa residues), rV-Msp (57 aa residues), and rN-Msp (272 aa residues), with

    Techniques Used: Recombinant

    Effect of exogenously added rMsp on adhesion of Treponema strains to immobilized human fibronectin or 30-kDa fibronectin fragment. (Panel A) Adhesion levels of T. denticola ATCC 35405 cells to 0.1 μg fibronectin (filled column) or 30-kDa fibronectin
    Figure Legend Snippet: Effect of exogenously added rMsp on adhesion of Treponema strains to immobilized human fibronectin or 30-kDa fibronectin fragment. (Panel A) Adhesion levels of T. denticola ATCC 35405 cells to 0.1 μg fibronectin (filled column) or 30-kDa fibronectin

    Techniques Used:

    11) Product Images from "Binding Properties and Adhesion-Mediating Regions of the Major Sheath Protein of Treponema denticola ATCC 35405"

    Article Title: Binding Properties and Adhesion-Mediating Regions of the Major Sheath Protein of Treponema denticola ATCC 35405

    Journal: Infection and Immunity

    doi: 10.1128/IAI.73.5.2891-2898.2005

    Interactions of rMsp antibodies with T. denticola ATCC 35405 cells and of whole-cell antibodies with rMsp fragments. (Panel A) Reactivity in ELISA of antiserum (1:250 diluted) to T. denticola ATCC 35405 cells (W) or antisera (1:250 diluted) raised to
    Figure Legend Snippet: Interactions of rMsp antibodies with T. denticola ATCC 35405 cells and of whole-cell antibodies with rMsp fragments. (Panel A) Reactivity in ELISA of antiserum (1:250 diluted) to T. denticola ATCC 35405 cells (W) or antisera (1:250 diluted) raised to

    Techniques Used: Enzyme-linked Immunosorbent Assay

    Reactivities of Msp antisera with T. denticola ATCC 35405 outer membrane protein extracts. (Panel A) SDS-PAGE gel of outer membrane proteins. (Panel B) Western blots reacted with antisera to rN-Msp (lane 1), rV-Msp (lane 2), or rC-Msp (lane 3). Molecular
    Figure Legend Snippet: Reactivities of Msp antisera with T. denticola ATCC 35405 outer membrane protein extracts. (Panel A) SDS-PAGE gel of outer membrane proteins. (Panel B) Western blots reacted with antisera to rN-Msp (lane 1), rV-Msp (lane 2), or rC-Msp (lane 3). Molecular

    Techniques Used: SDS Page, Western Blot

    Binding of rMsp to human fibronectin and to 30-kDa N-terminal fragment of human fibronectin. (Panel A) Western blot overlay of trypsin-derived fragments of human plasma fibronectin reacted with rMsp (lane 1) or with biotinylated T. denticola ATCC 35405
    Figure Legend Snippet: Binding of rMsp to human fibronectin and to 30-kDa N-terminal fragment of human fibronectin. (Panel A) Western blot overlay of trypsin-derived fragments of human plasma fibronectin reacted with rMsp (lane 1) or with biotinylated T. denticola ATCC 35405

    Techniques Used: Binding Assay, Western Blot, Derivative Assay

    Diagrammatic representation of the Msp sequences from T. denticola ATCC 35520 (A), strain ATCC 35405 (B), and of recombinant Msp polypeptides rMsp (530 aa residues), rN-Msp (189 aa residues), rV-Msp (57 aa residues), and rN-Msp (272 aa residues), with
    Figure Legend Snippet: Diagrammatic representation of the Msp sequences from T. denticola ATCC 35520 (A), strain ATCC 35405 (B), and of recombinant Msp polypeptides rMsp (530 aa residues), rN-Msp (189 aa residues), rV-Msp (57 aa residues), and rN-Msp (272 aa residues), with

    Techniques Used: Recombinant

    Effect of exogenously added rMsp on adhesion of Treponema strains to immobilized human fibronectin or 30-kDa fibronectin fragment. (Panel A) Adhesion levels of T. denticola ATCC 35405 cells to 0.1 μg fibronectin (filled column) or 30-kDa fibronectin
    Figure Legend Snippet: Effect of exogenously added rMsp on adhesion of Treponema strains to immobilized human fibronectin or 30-kDa fibronectin fragment. (Panel A) Adhesion levels of T. denticola ATCC 35405 cells to 0.1 μg fibronectin (filled column) or 30-kDa fibronectin

    Techniques Used:

    12) Product Images from "Dentilisin Activity Affects the Organization of the Outer Sheath of Treponema denticola"

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

    Journal: Journal of Bacteriology

    doi:

    Mean areas of lesions at infection sites after challenge with T. denticola ATCC 35405 and prtP mutant K1. Mice were injected with live T. denticola ATCC 35405 (open bars) or mutant K1 (hatched bars), and lesion areas were determined at the indicated times following infection.
    Figure Legend Snippet: Mean areas of lesions at infection sites after challenge with T. denticola ATCC 35405 and prtP mutant K1. Mice were injected with live T. denticola ATCC 35405 (open bars) or mutant K1 (hatched bars), and lesion areas were determined at the indicated times following infection.

    Techniques Used: Infection, Mutagenesis, Mouse Assay, Injection

    Immunoblot analysis of T. denticola ATCC 35405 and K1 with anti- T. denticola ATCC 35405 whole-cell serum. Samples from lanes 1 to 4 were treated with PMSF. Lanes 1 and 5, T. denticola ATCC 35405 (without boiling); lanes 2 and 6, T. denticola K1 (without boiling); lanes 3 and 7, T. denticola ATCC 35405 (with boiling); lanes 4 and 8, T. denticola K1 (with boiling). Arrowheads indicate the high-molecular-mass oligomeric protein and the Msp band.
    Figure Legend Snippet: Immunoblot analysis of T. denticola ATCC 35405 and K1 with anti- T. denticola ATCC 35405 whole-cell serum. Samples from lanes 1 to 4 were treated with PMSF. Lanes 1 and 5, T. denticola ATCC 35405 (without boiling); lanes 2 and 6, T. denticola K1 (without boiling); lanes 3 and 7, T. denticola ATCC 35405 (with boiling); lanes 4 and 8, T. denticola K1 (with boiling). Arrowheads indicate the high-molecular-mass oligomeric protein and the Msp band.

    Techniques Used:

    Southern blot analysis of T. denticola ATCC 35405 and prtP mutant K1. Chromosomal DNAs from T. denticola ATCC 35405 (lanes 1 and 3) and prtP mutant K1 (lanes 2 and 4) were digested with Hin dIII and hybridized with a digoxigenin-labeled Kpn I- Pst I fragment from the prtP gene (lanes 1 and 2) or the Kpn I- Bam HI fragment from pVA2198 (lanes 3 and 4). Numbers at right are kilobase pairs.
    Figure Legend Snippet: Southern blot analysis of T. denticola ATCC 35405 and prtP mutant K1. Chromosomal DNAs from T. denticola ATCC 35405 (lanes 1 and 3) and prtP mutant K1 (lanes 2 and 4) were digested with Hin dIII and hybridized with a digoxigenin-labeled Kpn I- Pst I fragment from the prtP gene (lanes 1 and 2) or the Kpn I- Bam HI fragment from pVA2198 (lanes 3 and 4). Numbers at right are kilobase pairs.

    Techniques Used: Southern Blot, Mutagenesis, Labeling

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

    Techniques Used: Zymography

    SDS-PAGE analysis of sonicates of T. denticola ATCC 35405 and K1. Samples from lanes 1 to 4 were treated with PMSF. Lanes 1 and 5, T. denticola ATCC 35405 (without boiling); lanes 2 and 6, T. denticola K1 (without boiling); lanes 3 and 7, T. denticola ATCC 35405 (with boiling); lanes 4 and 8, T. denticola K1 (with boiling). After electrophoresis, the gel was stained with Coomassie brilliant blue R-250. Arrowheads indicate the high-molecular-mass oligomeric protein and the Msp band.
    Figure Legend Snippet: SDS-PAGE analysis of sonicates of T. denticola ATCC 35405 and K1. Samples from lanes 1 to 4 were treated with PMSF. Lanes 1 and 5, T. denticola ATCC 35405 (without boiling); lanes 2 and 6, T. denticola K1 (without boiling); lanes 3 and 7, T. denticola ATCC 35405 (with boiling); lanes 4 and 8, T. denticola K1 (with boiling). After electrophoresis, the gel was stained with Coomassie brilliant blue R-250. Arrowheads indicate the high-molecular-mass oligomeric protein and the Msp band.

    Techniques Used: SDS Page, Electrophoresis, Staining

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

    Techniques Used:

    13) Product Images from "Dentilisin Activity Affects the Organization of the Outer Sheath of Treponema denticola"

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

    Journal: Journal of Bacteriology

    doi:

    Mean areas of lesions at infection sites after challenge with T. denticola ATCC 35405 and prtP mutant K1. Mice were injected with live T. denticola ATCC 35405 (open bars) or mutant K1 (hatched bars), and lesion areas were determined at the indicated times following infection.
    Figure Legend Snippet: Mean areas of lesions at infection sites after challenge with T. denticola ATCC 35405 and prtP mutant K1. Mice were injected with live T. denticola ATCC 35405 (open bars) or mutant K1 (hatched bars), and lesion areas were determined at the indicated times following infection.

    Techniques Used: Infection, Mutagenesis, Mouse Assay, Injection

    Immunoblot analysis of T. denticola ATCC 35405 and K1 with anti- T. denticola ATCC 35405 whole-cell serum. Samples from lanes 1 to 4 were treated with PMSF. Lanes 1 and 5, T. denticola ATCC 35405 (without boiling); lanes 2 and 6, T. denticola K1 (without boiling); lanes 3 and 7, T. denticola ATCC 35405 (with boiling); lanes 4 and 8, T. denticola K1 (with boiling). Arrowheads indicate the high-molecular-mass oligomeric protein and the Msp band.
    Figure Legend Snippet: Immunoblot analysis of T. denticola ATCC 35405 and K1 with anti- T. denticola ATCC 35405 whole-cell serum. Samples from lanes 1 to 4 were treated with PMSF. Lanes 1 and 5, T. denticola ATCC 35405 (without boiling); lanes 2 and 6, T. denticola K1 (without boiling); lanes 3 and 7, T. denticola ATCC 35405 (with boiling); lanes 4 and 8, T. denticola K1 (with boiling). Arrowheads indicate the high-molecular-mass oligomeric protein and the Msp band.

    Techniques Used:

    Southern blot analysis of T. denticola ATCC 35405 and prtP mutant K1. Chromosomal DNAs from T. denticola ATCC 35405 (lanes 1 and 3) and prtP mutant K1 (lanes 2 and 4) were digested with Hin dIII and hybridized with a digoxigenin-labeled Kpn I- Pst I fragment from the prtP gene (lanes 1 and 2) or the Kpn I- Bam HI fragment from pVA2198 (lanes 3 and 4). Numbers at right are kilobase pairs.
    Figure Legend Snippet: Southern blot analysis of T. denticola ATCC 35405 and prtP mutant K1. Chromosomal DNAs from T. denticola ATCC 35405 (lanes 1 and 3) and prtP mutant K1 (lanes 2 and 4) were digested with Hin dIII and hybridized with a digoxigenin-labeled Kpn I- Pst I fragment from the prtP gene (lanes 1 and 2) or the Kpn I- Bam HI fragment from pVA2198 (lanes 3 and 4). Numbers at right are kilobase pairs.

    Techniques Used: Southern Blot, Mutagenesis, Labeling

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

    Techniques Used: Zymography

    SDS-PAGE analysis of sonicates of T. denticola ATCC 35405 and K1. Samples from lanes 1 to 4 were treated with PMSF. Lanes 1 and 5, T. denticola ATCC 35405 (without boiling); lanes 2 and 6, T. denticola K1 (without boiling); lanes 3 and 7, T. denticola ATCC 35405 (with boiling); lanes 4 and 8, T. denticola K1 (with boiling). After electrophoresis, the gel was stained with Coomassie brilliant blue R-250. Arrowheads indicate the high-molecular-mass oligomeric protein and the Msp band.
    Figure Legend Snippet: SDS-PAGE analysis of sonicates of T. denticola ATCC 35405 and K1. Samples from lanes 1 to 4 were treated with PMSF. Lanes 1 and 5, T. denticola ATCC 35405 (without boiling); lanes 2 and 6, T. denticola K1 (without boiling); lanes 3 and 7, T. denticola ATCC 35405 (with boiling); lanes 4 and 8, T. denticola K1 (with boiling). After electrophoresis, the gel was stained with Coomassie brilliant blue R-250. Arrowheads indicate the high-molecular-mass oligomeric protein and the Msp band.

    Techniques Used: SDS Page, Electrophoresis, Staining

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

    Techniques Used:

    14) Product Images from "Dentilisin Activity Affects the Organization of the Outer Sheath of Treponema denticola"

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

    Journal: Journal of Bacteriology

    doi:

    Mean areas of lesions at infection sites after challenge with T. denticola ATCC 35405 and prtP mutant K1. Mice were injected with live T. denticola ATCC 35405 (open bars) or mutant K1 (hatched bars), and lesion areas were determined at the indicated times following infection.
    Figure Legend Snippet: Mean areas of lesions at infection sites after challenge with T. denticola ATCC 35405 and prtP mutant K1. Mice were injected with live T. denticola ATCC 35405 (open bars) or mutant K1 (hatched bars), and lesion areas were determined at the indicated times following infection.

    Techniques Used: Infection, Mutagenesis, Mouse Assay, Injection

    Immunoblot analysis of T. denticola ATCC 35405 and K1 with anti- T. denticola ATCC 35405 whole-cell serum. Samples from lanes 1 to 4 were treated with PMSF. Lanes 1 and 5, T. denticola ATCC 35405 (without boiling); lanes 2 and 6, T. denticola K1 (without boiling); lanes 3 and 7, T. denticola ATCC 35405 (with boiling); lanes 4 and 8, T. denticola K1 (with boiling). Arrowheads indicate the high-molecular-mass oligomeric protein and the Msp band.
    Figure Legend Snippet: Immunoblot analysis of T. denticola ATCC 35405 and K1 with anti- T. denticola ATCC 35405 whole-cell serum. Samples from lanes 1 to 4 were treated with PMSF. Lanes 1 and 5, T. denticola ATCC 35405 (without boiling); lanes 2 and 6, T. denticola K1 (without boiling); lanes 3 and 7, T. denticola ATCC 35405 (with boiling); lanes 4 and 8, T. denticola K1 (with boiling). Arrowheads indicate the high-molecular-mass oligomeric protein and the Msp band.

    Techniques Used:

    Southern blot analysis of T. denticola ATCC 35405 and prtP mutant K1. Chromosomal DNAs from T. denticola ATCC 35405 (lanes 1 and 3) and prtP mutant K1 (lanes 2 and 4) were digested with Hin dIII and hybridized with a digoxigenin-labeled Kpn I- Pst I fragment from the prtP gene (lanes 1 and 2) or the Kpn I- Bam HI fragment from pVA2198 (lanes 3 and 4). Numbers at right are kilobase pairs.
    Figure Legend Snippet: Southern blot analysis of T. denticola ATCC 35405 and prtP mutant K1. Chromosomal DNAs from T. denticola ATCC 35405 (lanes 1 and 3) and prtP mutant K1 (lanes 2 and 4) were digested with Hin dIII and hybridized with a digoxigenin-labeled Kpn I- Pst I fragment from the prtP gene (lanes 1 and 2) or the Kpn I- Bam HI fragment from pVA2198 (lanes 3 and 4). Numbers at right are kilobase pairs.

    Techniques Used: Southern Blot, Mutagenesis, Labeling

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

    Techniques Used: Zymography

    SDS-PAGE analysis of sonicates of T. denticola ATCC 35405 and K1. Samples from lanes 1 to 4 were treated with PMSF. Lanes 1 and 5, T. denticola ATCC 35405 (without boiling); lanes 2 and 6, T. denticola K1 (without boiling); lanes 3 and 7, T. denticola ATCC 35405 (with boiling); lanes 4 and 8, T. denticola K1 (with boiling). After electrophoresis, the gel was stained with Coomassie brilliant blue R-250. Arrowheads indicate the high-molecular-mass oligomeric protein and the Msp band.
    Figure Legend Snippet: SDS-PAGE analysis of sonicates of T. denticola ATCC 35405 and K1. Samples from lanes 1 to 4 were treated with PMSF. Lanes 1 and 5, T. denticola ATCC 35405 (without boiling); lanes 2 and 6, T. denticola K1 (without boiling); lanes 3 and 7, T. denticola ATCC 35405 (with boiling); lanes 4 and 8, T. denticola K1 (with boiling). After electrophoresis, the gel was stained with Coomassie brilliant blue R-250. Arrowheads indicate the high-molecular-mass oligomeric protein and the Msp band.

    Techniques Used: SDS Page, Electrophoresis, Staining

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

    Techniques Used:

    15) Product Images from "Dentilisin Activity Affects the Organization of the Outer Sheath of Treponema denticola"

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

    Journal: Journal of Bacteriology

    doi:

    Mean areas of lesions at infection sites after challenge with T. denticola ATCC 35405 and prtP mutant K1. Mice were injected with live T. denticola ATCC 35405 (open bars) or mutant K1 (hatched bars), and lesion areas were determined at the indicated times following infection.
    Figure Legend Snippet: Mean areas of lesions at infection sites after challenge with T. denticola ATCC 35405 and prtP mutant K1. Mice were injected with live T. denticola ATCC 35405 (open bars) or mutant K1 (hatched bars), and lesion areas were determined at the indicated times following infection.

    Techniques Used: Infection, Mutagenesis, Mouse Assay, Injection

    Immunoblot analysis of T. denticola ATCC 35405 and K1 with anti- T. denticola ATCC 35405 whole-cell serum. Samples from lanes 1 to 4 were treated with PMSF. Lanes 1 and 5, T. denticola ATCC 35405 (without boiling); lanes 2 and 6, T. denticola K1 (without boiling); lanes 3 and 7, T. denticola ATCC 35405 (with boiling); lanes 4 and 8, T. denticola K1 (with boiling). Arrowheads indicate the high-molecular-mass oligomeric protein and the Msp band.
    Figure Legend Snippet: Immunoblot analysis of T. denticola ATCC 35405 and K1 with anti- T. denticola ATCC 35405 whole-cell serum. Samples from lanes 1 to 4 were treated with PMSF. Lanes 1 and 5, T. denticola ATCC 35405 (without boiling); lanes 2 and 6, T. denticola K1 (without boiling); lanes 3 and 7, T. denticola ATCC 35405 (with boiling); lanes 4 and 8, T. denticola K1 (with boiling). Arrowheads indicate the high-molecular-mass oligomeric protein and the Msp band.

    Techniques Used:

    Southern blot analysis of T. denticola ATCC 35405 and prtP mutant K1. Chromosomal DNAs from T. denticola ATCC 35405 (lanes 1 and 3) and prtP mutant K1 (lanes 2 and 4) were digested with Hin dIII and hybridized with a digoxigenin-labeled Kpn I- Pst I fragment from the prtP gene (lanes 1 and 2) or the Kpn I- Bam HI fragment from pVA2198 (lanes 3 and 4). Numbers at right are kilobase pairs.
    Figure Legend Snippet: Southern blot analysis of T. denticola ATCC 35405 and prtP mutant K1. Chromosomal DNAs from T. denticola ATCC 35405 (lanes 1 and 3) and prtP mutant K1 (lanes 2 and 4) were digested with Hin dIII and hybridized with a digoxigenin-labeled Kpn I- Pst I fragment from the prtP gene (lanes 1 and 2) or the Kpn I- Bam HI fragment from pVA2198 (lanes 3 and 4). Numbers at right are kilobase pairs.

    Techniques Used: Southern Blot, Mutagenesis, Labeling

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

    Techniques Used: Zymography

    SDS-PAGE analysis of sonicates of T. denticola ATCC 35405 and K1. Samples from lanes 1 to 4 were treated with PMSF. Lanes 1 and 5, T. denticola ATCC 35405 (without boiling); lanes 2 and 6, T. denticola K1 (without boiling); lanes 3 and 7, T. denticola ATCC 35405 (with boiling); lanes 4 and 8, T. denticola K1 (with boiling). After electrophoresis, the gel was stained with Coomassie brilliant blue R-250. Arrowheads indicate the high-molecular-mass oligomeric protein and the Msp band.
    Figure Legend Snippet: SDS-PAGE analysis of sonicates of T. denticola ATCC 35405 and K1. Samples from lanes 1 to 4 were treated with PMSF. Lanes 1 and 5, T. denticola ATCC 35405 (without boiling); lanes 2 and 6, T. denticola K1 (without boiling); lanes 3 and 7, T. denticola ATCC 35405 (with boiling); lanes 4 and 8, T. denticola K1 (with boiling). After electrophoresis, the gel was stained with Coomassie brilliant blue R-250. Arrowheads indicate the high-molecular-mass oligomeric protein and the Msp band.

    Techniques Used: SDS Page, Electrophoresis, Staining

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

    Techniques Used:

    16) Product Images from "Dentilisin Activity Affects the Organization of the Outer Sheath of Treponema denticola"

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

    Journal: Journal of Bacteriology

    doi:

    Mean areas of lesions at infection sites after challenge with T. denticola ATCC 35405 and prtP mutant K1. Mice were injected with live T. denticola ATCC 35405 (open bars) or mutant K1 (hatched bars), and lesion areas were determined at the indicated times following infection.
    Figure Legend Snippet: Mean areas of lesions at infection sites after challenge with T. denticola ATCC 35405 and prtP mutant K1. Mice were injected with live T. denticola ATCC 35405 (open bars) or mutant K1 (hatched bars), and lesion areas were determined at the indicated times following infection.

    Techniques Used: Infection, Mutagenesis, Mouse Assay, Injection

    Immunoblot analysis of T. denticola ATCC 35405 and K1 with anti- T. denticola ATCC 35405 whole-cell serum. Samples from lanes 1 to 4 were treated with PMSF. Lanes 1 and 5, T. denticola ATCC 35405 (without boiling); lanes 2 and 6, T. denticola K1 (without boiling); lanes 3 and 7, T. denticola ATCC 35405 (with boiling); lanes 4 and 8, T. denticola K1 (with boiling). Arrowheads indicate the high-molecular-mass oligomeric protein and the Msp band.
    Figure Legend Snippet: Immunoblot analysis of T. denticola ATCC 35405 and K1 with anti- T. denticola ATCC 35405 whole-cell serum. Samples from lanes 1 to 4 were treated with PMSF. Lanes 1 and 5, T. denticola ATCC 35405 (without boiling); lanes 2 and 6, T. denticola K1 (without boiling); lanes 3 and 7, T. denticola ATCC 35405 (with boiling); lanes 4 and 8, T. denticola K1 (with boiling). Arrowheads indicate the high-molecular-mass oligomeric protein and the Msp band.

    Techniques Used:

    Southern blot analysis of T. denticola ATCC 35405 and prtP mutant K1. Chromosomal DNAs from T. denticola ATCC 35405 (lanes 1 and 3) and prtP mutant K1 (lanes 2 and 4) were digested with Hin dIII and hybridized with a digoxigenin-labeled Kpn I- Pst I fragment from the prtP gene (lanes 1 and 2) or the Kpn I- Bam HI fragment from pVA2198 (lanes 3 and 4). Numbers at right are kilobase pairs.
    Figure Legend Snippet: Southern blot analysis of T. denticola ATCC 35405 and prtP mutant K1. Chromosomal DNAs from T. denticola ATCC 35405 (lanes 1 and 3) and prtP mutant K1 (lanes 2 and 4) were digested with Hin dIII and hybridized with a digoxigenin-labeled Kpn I- Pst I fragment from the prtP gene (lanes 1 and 2) or the Kpn I- Bam HI fragment from pVA2198 (lanes 3 and 4). Numbers at right are kilobase pairs.

    Techniques Used: Southern Blot, Mutagenesis, Labeling

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

    Techniques Used: Zymography

    SDS-PAGE analysis of sonicates of T. denticola ATCC 35405 and K1. Samples from lanes 1 to 4 were treated with PMSF. Lanes 1 and 5, T. denticola ATCC 35405 (without boiling); lanes 2 and 6, T. denticola K1 (without boiling); lanes 3 and 7, T. denticola ATCC 35405 (with boiling); lanes 4 and 8, T. denticola K1 (with boiling). After electrophoresis, the gel was stained with Coomassie brilliant blue R-250. Arrowheads indicate the high-molecular-mass oligomeric protein and the Msp band.
    Figure Legend Snippet: SDS-PAGE analysis of sonicates of T. denticola ATCC 35405 and K1. Samples from lanes 1 to 4 were treated with PMSF. Lanes 1 and 5, T. denticola ATCC 35405 (without boiling); lanes 2 and 6, T. denticola K1 (without boiling); lanes 3 and 7, T. denticola ATCC 35405 (with boiling); lanes 4 and 8, T. denticola K1 (with boiling). After electrophoresis, the gel was stained with Coomassie brilliant blue R-250. Arrowheads indicate the high-molecular-mass oligomeric protein and the Msp band.

    Techniques Used: SDS Page, Electrophoresis, Staining

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

    Techniques Used:

    17) Product Images from "Dentilisin Activity Affects the Organization of the Outer Sheath of Treponema denticola"

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

    Journal: Journal of Bacteriology

    doi:

    Mean areas of lesions at infection sites after challenge with T. denticola ATCC 35405 and prtP mutant K1. Mice were injected with live T. denticola ATCC 35405 (open bars) or mutant K1 (hatched bars), and lesion areas were determined at the indicated times following infection.
    Figure Legend Snippet: Mean areas of lesions at infection sites after challenge with T. denticola ATCC 35405 and prtP mutant K1. Mice were injected with live T. denticola ATCC 35405 (open bars) or mutant K1 (hatched bars), and lesion areas were determined at the indicated times following infection.

    Techniques Used: Infection, Mutagenesis, Mouse Assay, Injection

    Immunoblot analysis of T. denticola ATCC 35405 and K1 with anti- T. denticola ATCC 35405 whole-cell serum. Samples from lanes 1 to 4 were treated with PMSF. Lanes 1 and 5, T. denticola ATCC 35405 (without boiling); lanes 2 and 6, T. denticola K1 (without boiling); lanes 3 and 7, T. denticola ATCC 35405 (with boiling); lanes 4 and 8, T. denticola K1 (with boiling). Arrowheads indicate the high-molecular-mass oligomeric protein and the Msp band.
    Figure Legend Snippet: Immunoblot analysis of T. denticola ATCC 35405 and K1 with anti- T. denticola ATCC 35405 whole-cell serum. Samples from lanes 1 to 4 were treated with PMSF. Lanes 1 and 5, T. denticola ATCC 35405 (without boiling); lanes 2 and 6, T. denticola K1 (without boiling); lanes 3 and 7, T. denticola ATCC 35405 (with boiling); lanes 4 and 8, T. denticola K1 (with boiling). Arrowheads indicate the high-molecular-mass oligomeric protein and the Msp band.

    Techniques Used:

    Southern blot analysis of T. denticola ATCC 35405 and prtP mutant K1. Chromosomal DNAs from T. denticola ATCC 35405 (lanes 1 and 3) and prtP mutant K1 (lanes 2 and 4) were digested with Hin dIII and hybridized with a digoxigenin-labeled Kpn I- Pst I fragment from the prtP gene (lanes 1 and 2) or the Kpn I- Bam HI fragment from pVA2198 (lanes 3 and 4). Numbers at right are kilobase pairs.
    Figure Legend Snippet: Southern blot analysis of T. denticola ATCC 35405 and prtP mutant K1. Chromosomal DNAs from T. denticola ATCC 35405 (lanes 1 and 3) and prtP mutant K1 (lanes 2 and 4) were digested with Hin dIII and hybridized with a digoxigenin-labeled Kpn I- Pst I fragment from the prtP gene (lanes 1 and 2) or the Kpn I- Bam HI fragment from pVA2198 (lanes 3 and 4). Numbers at right are kilobase pairs.

    Techniques Used: Southern Blot, Mutagenesis, Labeling

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

    Techniques Used: Zymography

    SDS-PAGE analysis of sonicates of T. denticola ATCC 35405 and K1. Samples from lanes 1 to 4 were treated with PMSF. Lanes 1 and 5, T. denticola ATCC 35405 (without boiling); lanes 2 and 6, T. denticola K1 (without boiling); lanes 3 and 7, T. denticola ATCC 35405 (with boiling); lanes 4 and 8, T. denticola K1 (with boiling). After electrophoresis, the gel was stained with Coomassie brilliant blue R-250. Arrowheads indicate the high-molecular-mass oligomeric protein and the Msp band.
    Figure Legend Snippet: SDS-PAGE analysis of sonicates of T. denticola ATCC 35405 and K1. Samples from lanes 1 to 4 were treated with PMSF. Lanes 1 and 5, T. denticola ATCC 35405 (without boiling); lanes 2 and 6, T. denticola K1 (without boiling); lanes 3 and 7, T. denticola ATCC 35405 (with boiling); lanes 4 and 8, T. denticola K1 (with boiling). After electrophoresis, the gel was stained with Coomassie brilliant blue R-250. Arrowheads indicate the high-molecular-mass oligomeric protein and the Msp band.

    Techniques Used: SDS Page, Electrophoresis, Staining

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

    Techniques Used:

    18) Product Images from "Dentilisin Activity Affects the Organization of the Outer Sheath of Treponema denticola"

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

    Journal: Journal of Bacteriology

    doi:

    Mean areas of lesions at infection sites after challenge with T. denticola ATCC 35405 and prtP mutant K1. Mice were injected with live T. denticola ATCC 35405 (open bars) or mutant K1 (hatched bars), and lesion areas were determined at the indicated times following infection.
    Figure Legend Snippet: Mean areas of lesions at infection sites after challenge with T. denticola ATCC 35405 and prtP mutant K1. Mice were injected with live T. denticola ATCC 35405 (open bars) or mutant K1 (hatched bars), and lesion areas were determined at the indicated times following infection.

    Techniques Used: Infection, Mutagenesis, Mouse Assay, Injection

    Immunoblot analysis of T. denticola ATCC 35405 and K1 with anti- T. denticola ATCC 35405 whole-cell serum. Samples from lanes 1 to 4 were treated with PMSF. Lanes 1 and 5, T. denticola ATCC 35405 (without boiling); lanes 2 and 6, T. denticola K1 (without boiling); lanes 3 and 7, T. denticola ATCC 35405 (with boiling); lanes 4 and 8, T. denticola K1 (with boiling). Arrowheads indicate the high-molecular-mass oligomeric protein and the Msp band.
    Figure Legend Snippet: Immunoblot analysis of T. denticola ATCC 35405 and K1 with anti- T. denticola ATCC 35405 whole-cell serum. Samples from lanes 1 to 4 were treated with PMSF. Lanes 1 and 5, T. denticola ATCC 35405 (without boiling); lanes 2 and 6, T. denticola K1 (without boiling); lanes 3 and 7, T. denticola ATCC 35405 (with boiling); lanes 4 and 8, T. denticola K1 (with boiling). Arrowheads indicate the high-molecular-mass oligomeric protein and the Msp band.

    Techniques Used:

    Southern blot analysis of T. denticola ATCC 35405 and prtP mutant K1. Chromosomal DNAs from T. denticola ATCC 35405 (lanes 1 and 3) and prtP mutant K1 (lanes 2 and 4) were digested with Hin dIII and hybridized with a digoxigenin-labeled Kpn I- Pst I fragment from the prtP gene (lanes 1 and 2) or the Kpn I- Bam HI fragment from pVA2198 (lanes 3 and 4). Numbers at right are kilobase pairs.
    Figure Legend Snippet: Southern blot analysis of T. denticola ATCC 35405 and prtP mutant K1. Chromosomal DNAs from T. denticola ATCC 35405 (lanes 1 and 3) and prtP mutant K1 (lanes 2 and 4) were digested with Hin dIII and hybridized with a digoxigenin-labeled Kpn I- Pst I fragment from the prtP gene (lanes 1 and 2) or the Kpn I- Bam HI fragment from pVA2198 (lanes 3 and 4). Numbers at right are kilobase pairs.

    Techniques Used: Southern Blot, Mutagenesis, Labeling

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

    Techniques Used: Zymography

    SDS-PAGE analysis of sonicates of T. denticola ATCC 35405 and K1. Samples from lanes 1 to 4 were treated with PMSF. Lanes 1 and 5, T. denticola ATCC 35405 (without boiling); lanes 2 and 6, T. denticola K1 (without boiling); lanes 3 and 7, T. denticola ATCC 35405 (with boiling); lanes 4 and 8, T. denticola K1 (with boiling). After electrophoresis, the gel was stained with Coomassie brilliant blue R-250. Arrowheads indicate the high-molecular-mass oligomeric protein and the Msp band.
    Figure Legend Snippet: SDS-PAGE analysis of sonicates of T. denticola ATCC 35405 and K1. Samples from lanes 1 to 4 were treated with PMSF. Lanes 1 and 5, T. denticola ATCC 35405 (without boiling); lanes 2 and 6, T. denticola K1 (without boiling); lanes 3 and 7, T. denticola ATCC 35405 (with boiling); lanes 4 and 8, T. denticola K1 (with boiling). After electrophoresis, the gel was stained with Coomassie brilliant blue R-250. Arrowheads indicate the high-molecular-mass oligomeric protein and the Msp band.

    Techniques Used: SDS Page, Electrophoresis, Staining

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

    Techniques Used:

    19) Product Images from "Dentilisin Activity Affects the Organization of the Outer Sheath of Treponema denticola"

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

    Journal: Journal of Bacteriology

    doi:

    Mean areas of lesions at infection sites after challenge with T. denticola ATCC 35405 and prtP mutant K1. Mice were injected with live T. denticola ATCC 35405 (open bars) or mutant K1 (hatched bars), and lesion areas were determined at the indicated times following infection.
    Figure Legend Snippet: Mean areas of lesions at infection sites after challenge with T. denticola ATCC 35405 and prtP mutant K1. Mice were injected with live T. denticola ATCC 35405 (open bars) or mutant K1 (hatched bars), and lesion areas were determined at the indicated times following infection.

    Techniques Used: Infection, Mutagenesis, Mouse Assay, Injection

    Immunoblot analysis of T. denticola ATCC 35405 and K1 with anti- T. denticola ATCC 35405 whole-cell serum. Samples from lanes 1 to 4 were treated with PMSF. Lanes 1 and 5, T. denticola ATCC 35405 (without boiling); lanes 2 and 6, T. denticola K1 (without boiling); lanes 3 and 7, T. denticola ATCC 35405 (with boiling); lanes 4 and 8, T. denticola K1 (with boiling). Arrowheads indicate the high-molecular-mass oligomeric protein and the Msp band.
    Figure Legend Snippet: Immunoblot analysis of T. denticola ATCC 35405 and K1 with anti- T. denticola ATCC 35405 whole-cell serum. Samples from lanes 1 to 4 were treated with PMSF. Lanes 1 and 5, T. denticola ATCC 35405 (without boiling); lanes 2 and 6, T. denticola K1 (without boiling); lanes 3 and 7, T. denticola ATCC 35405 (with boiling); lanes 4 and 8, T. denticola K1 (with boiling). Arrowheads indicate the high-molecular-mass oligomeric protein and the Msp band.

    Techniques Used:

    Southern blot analysis of T. denticola ATCC 35405 and prtP mutant K1. Chromosomal DNAs from T. denticola ATCC 35405 (lanes 1 and 3) and prtP mutant K1 (lanes 2 and 4) were digested with Hin dIII and hybridized with a digoxigenin-labeled Kpn I- Pst I fragment from the prtP gene (lanes 1 and 2) or the Kpn I- Bam HI fragment from pVA2198 (lanes 3 and 4). Numbers at right are kilobase pairs.
    Figure Legend Snippet: Southern blot analysis of T. denticola ATCC 35405 and prtP mutant K1. Chromosomal DNAs from T. denticola ATCC 35405 (lanes 1 and 3) and prtP mutant K1 (lanes 2 and 4) were digested with Hin dIII and hybridized with a digoxigenin-labeled Kpn I- Pst I fragment from the prtP gene (lanes 1 and 2) or the Kpn I- Bam HI fragment from pVA2198 (lanes 3 and 4). Numbers at right are kilobase pairs.

    Techniques Used: Southern Blot, Mutagenesis, Labeling

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

    Techniques Used: Zymography

    SDS-PAGE analysis of sonicates of T. denticola ATCC 35405 and K1. Samples from lanes 1 to 4 were treated with PMSF. Lanes 1 and 5, T. denticola ATCC 35405 (without boiling); lanes 2 and 6, T. denticola K1 (without boiling); lanes 3 and 7, T. denticola ATCC 35405 (with boiling); lanes 4 and 8, T. denticola K1 (with boiling). After electrophoresis, the gel was stained with Coomassie brilliant blue R-250. Arrowheads indicate the high-molecular-mass oligomeric protein and the Msp band.
    Figure Legend Snippet: SDS-PAGE analysis of sonicates of T. denticola ATCC 35405 and K1. Samples from lanes 1 to 4 were treated with PMSF. Lanes 1 and 5, T. denticola ATCC 35405 (without boiling); lanes 2 and 6, T. denticola K1 (without boiling); lanes 3 and 7, T. denticola ATCC 35405 (with boiling); lanes 4 and 8, T. denticola K1 (with boiling). After electrophoresis, the gel was stained with Coomassie brilliant blue R-250. Arrowheads indicate the high-molecular-mass oligomeric protein and the Msp band.

    Techniques Used: SDS Page, Electrophoresis, Staining

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

    Techniques Used:

    20) Product Images from "Binding Properties and Adhesion-Mediating Regions of the Major Sheath Protein of Treponema denticola ATCC 35405"

    Article Title: Binding Properties and Adhesion-Mediating Regions of the Major Sheath Protein of Treponema denticola ATCC 35405

    Journal: Infection and Immunity

    doi: 10.1128/IAI.73.5.2891-2898.2005

    Interactions of rMsp antibodies with T. denticola ATCC 35405 cells and of whole-cell antibodies with rMsp fragments. (Panel A) Reactivity in ELISA of antiserum (1:250 diluted) to T. denticola ATCC 35405 cells (W) or antisera (1:250 diluted) raised to
    Figure Legend Snippet: Interactions of rMsp antibodies with T. denticola ATCC 35405 cells and of whole-cell antibodies with rMsp fragments. (Panel A) Reactivity in ELISA of antiserum (1:250 diluted) to T. denticola ATCC 35405 cells (W) or antisera (1:250 diluted) raised to

    Techniques Used: Enzyme-linked Immunosorbent Assay

    Reactivities of Msp antisera with T. denticola ATCC 35405 outer membrane protein extracts. (Panel A) SDS-PAGE gel of outer membrane proteins. (Panel B) Western blots reacted with antisera to rN-Msp (lane 1), rV-Msp (lane 2), or rC-Msp (lane 3). Molecular
    Figure Legend Snippet: Reactivities of Msp antisera with T. denticola ATCC 35405 outer membrane protein extracts. (Panel A) SDS-PAGE gel of outer membrane proteins. (Panel B) Western blots reacted with antisera to rN-Msp (lane 1), rV-Msp (lane 2), or rC-Msp (lane 3). Molecular

    Techniques Used: SDS Page, Western Blot

    Binding of rMsp to human fibronectin and to 30-kDa N-terminal fragment of human fibronectin. (Panel A) Western blot overlay of trypsin-derived fragments of human plasma fibronectin reacted with rMsp (lane 1) or with biotinylated T. denticola ATCC 35405
    Figure Legend Snippet: Binding of rMsp to human fibronectin and to 30-kDa N-terminal fragment of human fibronectin. (Panel A) Western blot overlay of trypsin-derived fragments of human plasma fibronectin reacted with rMsp (lane 1) or with biotinylated T. denticola ATCC 35405

    Techniques Used: Binding Assay, Western Blot, Derivative Assay

    Diagrammatic representation of the Msp sequences from T. denticola ATCC 35520 (A), strain ATCC 35405 (B), and of recombinant Msp polypeptides rMsp (530 aa residues), rN-Msp (189 aa residues), rV-Msp (57 aa residues), and rN-Msp (272 aa residues), with
    Figure Legend Snippet: Diagrammatic representation of the Msp sequences from T. denticola ATCC 35520 (A), strain ATCC 35405 (B), and of recombinant Msp polypeptides rMsp (530 aa residues), rN-Msp (189 aa residues), rV-Msp (57 aa residues), and rN-Msp (272 aa residues), with

    Techniques Used: Recombinant

    Effect of exogenously added rMsp on adhesion of Treponema strains to immobilized human fibronectin or 30-kDa fibronectin fragment. (Panel A) Adhesion levels of T. denticola ATCC 35405 cells to 0.1 μg fibronectin (filled column) or 30-kDa fibronectin
    Figure Legend Snippet: Effect of exogenously added rMsp on adhesion of Treponema strains to immobilized human fibronectin or 30-kDa fibronectin fragment. (Panel A) Adhesion levels of T. denticola ATCC 35405 cells to 0.1 μg fibronectin (filled column) or 30-kDa fibronectin

    Techniques Used:

    21) Product Images from "Binding Properties and Adhesion-Mediating Regions of the Major Sheath Protein of Treponema denticola ATCC 35405"

    Article Title: Binding Properties and Adhesion-Mediating Regions of the Major Sheath Protein of Treponema denticola ATCC 35405

    Journal: Infection and Immunity

    doi: 10.1128/IAI.73.5.2891-2898.2005

    Interactions of rMsp antibodies with T. denticola ATCC 35405 cells and of whole-cell antibodies with rMsp fragments. (Panel A) Reactivity in ELISA of antiserum (1:250 diluted) to T. denticola ATCC 35405 cells (W) or antisera (1:250 diluted) raised to
    Figure Legend Snippet: Interactions of rMsp antibodies with T. denticola ATCC 35405 cells and of whole-cell antibodies with rMsp fragments. (Panel A) Reactivity in ELISA of antiserum (1:250 diluted) to T. denticola ATCC 35405 cells (W) or antisera (1:250 diluted) raised to

    Techniques Used: Enzyme-linked Immunosorbent Assay

    Reactivities of Msp antisera with T. denticola ATCC 35405 outer membrane protein extracts. (Panel A) SDS-PAGE gel of outer membrane proteins. (Panel B) Western blots reacted with antisera to rN-Msp (lane 1), rV-Msp (lane 2), or rC-Msp (lane 3). Molecular
    Figure Legend Snippet: Reactivities of Msp antisera with T. denticola ATCC 35405 outer membrane protein extracts. (Panel A) SDS-PAGE gel of outer membrane proteins. (Panel B) Western blots reacted with antisera to rN-Msp (lane 1), rV-Msp (lane 2), or rC-Msp (lane 3). Molecular

    Techniques Used: SDS Page, Western Blot

    Binding of rMsp to human fibronectin and to 30-kDa N-terminal fragment of human fibronectin. (Panel A) Western blot overlay of trypsin-derived fragments of human plasma fibronectin reacted with rMsp (lane 1) or with biotinylated T. denticola ATCC 35405
    Figure Legend Snippet: Binding of rMsp to human fibronectin and to 30-kDa N-terminal fragment of human fibronectin. (Panel A) Western blot overlay of trypsin-derived fragments of human plasma fibronectin reacted with rMsp (lane 1) or with biotinylated T. denticola ATCC 35405

    Techniques Used: Binding Assay, Western Blot, Derivative Assay

    Diagrammatic representation of the Msp sequences from T. denticola ATCC 35520 (A), strain ATCC 35405 (B), and of recombinant Msp polypeptides rMsp (530 aa residues), rN-Msp (189 aa residues), rV-Msp (57 aa residues), and rN-Msp (272 aa residues), with
    Figure Legend Snippet: Diagrammatic representation of the Msp sequences from T. denticola ATCC 35520 (A), strain ATCC 35405 (B), and of recombinant Msp polypeptides rMsp (530 aa residues), rN-Msp (189 aa residues), rV-Msp (57 aa residues), and rN-Msp (272 aa residues), with

    Techniques Used: Recombinant

    Effect of exogenously added rMsp on adhesion of Treponema strains to immobilized human fibronectin or 30-kDa fibronectin fragment. (Panel A) Adhesion levels of T. denticola ATCC 35405 cells to 0.1 μg fibronectin (filled column) or 30-kDa fibronectin
    Figure Legend Snippet: Effect of exogenously added rMsp on adhesion of Treponema strains to immobilized human fibronectin or 30-kDa fibronectin fragment. (Panel A) Adhesion levels of T. denticola ATCC 35405 cells to 0.1 μg fibronectin (filled column) or 30-kDa fibronectin

    Techniques Used:

    22) Product Images from "Binding Properties and Adhesion-Mediating Regions of the Major Sheath Protein of Treponema denticola ATCC 35405"

    Article Title: Binding Properties and Adhesion-Mediating Regions of the Major Sheath Protein of Treponema denticola ATCC 35405

    Journal: Infection and Immunity

    doi: 10.1128/IAI.73.5.2891-2898.2005

    Interactions of rMsp antibodies with T. denticola ATCC 35405 cells and of whole-cell antibodies with rMsp fragments. (Panel A) Reactivity in ELISA of antiserum (1:250 diluted) to T. denticola ATCC 35405 cells (W) or antisera (1:250 diluted) raised to
    Figure Legend Snippet: Interactions of rMsp antibodies with T. denticola ATCC 35405 cells and of whole-cell antibodies with rMsp fragments. (Panel A) Reactivity in ELISA of antiserum (1:250 diluted) to T. denticola ATCC 35405 cells (W) or antisera (1:250 diluted) raised to

    Techniques Used: Enzyme-linked Immunosorbent Assay

    Reactivities of Msp antisera with T. denticola ATCC 35405 outer membrane protein extracts. (Panel A) SDS-PAGE gel of outer membrane proteins. (Panel B) Western blots reacted with antisera to rN-Msp (lane 1), rV-Msp (lane 2), or rC-Msp (lane 3). Molecular
    Figure Legend Snippet: Reactivities of Msp antisera with T. denticola ATCC 35405 outer membrane protein extracts. (Panel A) SDS-PAGE gel of outer membrane proteins. (Panel B) Western blots reacted with antisera to rN-Msp (lane 1), rV-Msp (lane 2), or rC-Msp (lane 3). Molecular

    Techniques Used: SDS Page, Western Blot

    Binding of rMsp to human fibronectin and to 30-kDa N-terminal fragment of human fibronectin. (Panel A) Western blot overlay of trypsin-derived fragments of human plasma fibronectin reacted with rMsp (lane 1) or with biotinylated T. denticola ATCC 35405
    Figure Legend Snippet: Binding of rMsp to human fibronectin and to 30-kDa N-terminal fragment of human fibronectin. (Panel A) Western blot overlay of trypsin-derived fragments of human plasma fibronectin reacted with rMsp (lane 1) or with biotinylated T. denticola ATCC 35405

    Techniques Used: Binding Assay, Western Blot, Derivative Assay

    Diagrammatic representation of the Msp sequences from T. denticola ATCC 35520 (A), strain ATCC 35405 (B), and of recombinant Msp polypeptides rMsp (530 aa residues), rN-Msp (189 aa residues), rV-Msp (57 aa residues), and rN-Msp (272 aa residues), with
    Figure Legend Snippet: Diagrammatic representation of the Msp sequences from T. denticola ATCC 35520 (A), strain ATCC 35405 (B), and of recombinant Msp polypeptides rMsp (530 aa residues), rN-Msp (189 aa residues), rV-Msp (57 aa residues), and rN-Msp (272 aa residues), with

    Techniques Used: Recombinant

    Effect of exogenously added rMsp on adhesion of Treponema strains to immobilized human fibronectin or 30-kDa fibronectin fragment. (Panel A) Adhesion levels of T. denticola ATCC 35405 cells to 0.1 μg fibronectin (filled column) or 30-kDa fibronectin
    Figure Legend Snippet: Effect of exogenously added rMsp on adhesion of Treponema strains to immobilized human fibronectin or 30-kDa fibronectin fragment. (Panel A) Adhesion levels of T. denticola ATCC 35405 cells to 0.1 μg fibronectin (filled column) or 30-kDa fibronectin

    Techniques Used:

    23) Product Images from "Binding Properties and Adhesion-Mediating Regions of the Major Sheath Protein of Treponema denticola ATCC 35405"

    Article Title: Binding Properties and Adhesion-Mediating Regions of the Major Sheath Protein of Treponema denticola ATCC 35405

    Journal: Infection and Immunity

    doi: 10.1128/IAI.73.5.2891-2898.2005

    Interactions of rMsp antibodies with T. denticola ATCC 35405 cells and of whole-cell antibodies with rMsp fragments. (Panel A) Reactivity in ELISA of antiserum (1:250 diluted) to T. denticola ATCC 35405 cells (W) or antisera (1:250 diluted) raised to
    Figure Legend Snippet: Interactions of rMsp antibodies with T. denticola ATCC 35405 cells and of whole-cell antibodies with rMsp fragments. (Panel A) Reactivity in ELISA of antiserum (1:250 diluted) to T. denticola ATCC 35405 cells (W) or antisera (1:250 diluted) raised to

    Techniques Used: Enzyme-linked Immunosorbent Assay

    Reactivities of Msp antisera with T. denticola ATCC 35405 outer membrane protein extracts. (Panel A) SDS-PAGE gel of outer membrane proteins. (Panel B) Western blots reacted with antisera to rN-Msp (lane 1), rV-Msp (lane 2), or rC-Msp (lane 3). Molecular
    Figure Legend Snippet: Reactivities of Msp antisera with T. denticola ATCC 35405 outer membrane protein extracts. (Panel A) SDS-PAGE gel of outer membrane proteins. (Panel B) Western blots reacted with antisera to rN-Msp (lane 1), rV-Msp (lane 2), or rC-Msp (lane 3). Molecular

    Techniques Used: SDS Page, Western Blot

    Binding of rMsp to human fibronectin and to 30-kDa N-terminal fragment of human fibronectin. (Panel A) Western blot overlay of trypsin-derived fragments of human plasma fibronectin reacted with rMsp (lane 1) or with biotinylated T. denticola ATCC 35405
    Figure Legend Snippet: Binding of rMsp to human fibronectin and to 30-kDa N-terminal fragment of human fibronectin. (Panel A) Western blot overlay of trypsin-derived fragments of human plasma fibronectin reacted with rMsp (lane 1) or with biotinylated T. denticola ATCC 35405

    Techniques Used: Binding Assay, Western Blot, Derivative Assay

    Diagrammatic representation of the Msp sequences from T. denticola ATCC 35520 (A), strain ATCC 35405 (B), and of recombinant Msp polypeptides rMsp (530 aa residues), rN-Msp (189 aa residues), rV-Msp (57 aa residues), and rN-Msp (272 aa residues), with
    Figure Legend Snippet: Diagrammatic representation of the Msp sequences from T. denticola ATCC 35520 (A), strain ATCC 35405 (B), and of recombinant Msp polypeptides rMsp (530 aa residues), rN-Msp (189 aa residues), rV-Msp (57 aa residues), and rN-Msp (272 aa residues), with

    Techniques Used: Recombinant

    Effect of exogenously added rMsp on adhesion of Treponema strains to immobilized human fibronectin or 30-kDa fibronectin fragment. (Panel A) Adhesion levels of T. denticola ATCC 35405 cells to 0.1 μg fibronectin (filled column) or 30-kDa fibronectin
    Figure Legend Snippet: Effect of exogenously added rMsp on adhesion of Treponema strains to immobilized human fibronectin or 30-kDa fibronectin fragment. (Panel A) Adhesion levels of T. denticola ATCC 35405 cells to 0.1 μg fibronectin (filled column) or 30-kDa fibronectin

    Techniques Used:

    24) Product Images from "Binding Properties and Adhesion-Mediating Regions of the Major Sheath Protein of Treponema denticola ATCC 35405"

    Article Title: Binding Properties and Adhesion-Mediating Regions of the Major Sheath Protein of Treponema denticola ATCC 35405

    Journal: Infection and Immunity

    doi: 10.1128/IAI.73.5.2891-2898.2005

    Interactions of rMsp antibodies with T. denticola ATCC 35405 cells and of whole-cell antibodies with rMsp fragments. (Panel A) Reactivity in ELISA of antiserum (1:250 diluted) to T. denticola ATCC 35405 cells (W) or antisera (1:250 diluted) raised to
    Figure Legend Snippet: Interactions of rMsp antibodies with T. denticola ATCC 35405 cells and of whole-cell antibodies with rMsp fragments. (Panel A) Reactivity in ELISA of antiserum (1:250 diluted) to T. denticola ATCC 35405 cells (W) or antisera (1:250 diluted) raised to

    Techniques Used: Enzyme-linked Immunosorbent Assay

    Reactivities of Msp antisera with T. denticola ATCC 35405 outer membrane protein extracts. (Panel A) SDS-PAGE gel of outer membrane proteins. (Panel B) Western blots reacted with antisera to rN-Msp (lane 1), rV-Msp (lane 2), or rC-Msp (lane 3). Molecular
    Figure Legend Snippet: Reactivities of Msp antisera with T. denticola ATCC 35405 outer membrane protein extracts. (Panel A) SDS-PAGE gel of outer membrane proteins. (Panel B) Western blots reacted with antisera to rN-Msp (lane 1), rV-Msp (lane 2), or rC-Msp (lane 3). Molecular

    Techniques Used: SDS Page, Western Blot

    Binding of rMsp to human fibronectin and to 30-kDa N-terminal fragment of human fibronectin. (Panel A) Western blot overlay of trypsin-derived fragments of human plasma fibronectin reacted with rMsp (lane 1) or with biotinylated T. denticola ATCC 35405
    Figure Legend Snippet: Binding of rMsp to human fibronectin and to 30-kDa N-terminal fragment of human fibronectin. (Panel A) Western blot overlay of trypsin-derived fragments of human plasma fibronectin reacted with rMsp (lane 1) or with biotinylated T. denticola ATCC 35405

    Techniques Used: Binding Assay, Western Blot, Derivative Assay

    Diagrammatic representation of the Msp sequences from T. denticola ATCC 35520 (A), strain ATCC 35405 (B), and of recombinant Msp polypeptides rMsp (530 aa residues), rN-Msp (189 aa residues), rV-Msp (57 aa residues), and rN-Msp (272 aa residues), with
    Figure Legend Snippet: Diagrammatic representation of the Msp sequences from T. denticola ATCC 35520 (A), strain ATCC 35405 (B), and of recombinant Msp polypeptides rMsp (530 aa residues), rN-Msp (189 aa residues), rV-Msp (57 aa residues), and rN-Msp (272 aa residues), with

    Techniques Used: Recombinant

    Effect of exogenously added rMsp on adhesion of Treponema strains to immobilized human fibronectin or 30-kDa fibronectin fragment. (Panel A) Adhesion levels of T. denticola ATCC 35405 cells to 0.1 μg fibronectin (filled column) or 30-kDa fibronectin
    Figure Legend Snippet: Effect of exogenously added rMsp on adhesion of Treponema strains to immobilized human fibronectin or 30-kDa fibronectin fragment. (Panel A) Adhesion levels of T. denticola ATCC 35405 cells to 0.1 μg fibronectin (filled column) or 30-kDa fibronectin

    Techniques Used:

    25) Product Images from "Binding Properties and Adhesion-Mediating Regions of the Major Sheath Protein of Treponema denticola ATCC 35405"

    Article Title: Binding Properties and Adhesion-Mediating Regions of the Major Sheath Protein of Treponema denticola ATCC 35405

    Journal: Infection and Immunity

    doi: 10.1128/IAI.73.5.2891-2898.2005

    Interactions of rMsp antibodies with T. denticola ATCC 35405 cells and of whole-cell antibodies with rMsp fragments. (Panel A) Reactivity in ELISA of antiserum (1:250 diluted) to T. denticola ATCC 35405 cells (W) or antisera (1:250 diluted) raised to
    Figure Legend Snippet: Interactions of rMsp antibodies with T. denticola ATCC 35405 cells and of whole-cell antibodies with rMsp fragments. (Panel A) Reactivity in ELISA of antiserum (1:250 diluted) to T. denticola ATCC 35405 cells (W) or antisera (1:250 diluted) raised to

    Techniques Used: Enzyme-linked Immunosorbent Assay

    Reactivities of Msp antisera with T. denticola ATCC 35405 outer membrane protein extracts. (Panel A) SDS-PAGE gel of outer membrane proteins. (Panel B) Western blots reacted with antisera to rN-Msp (lane 1), rV-Msp (lane 2), or rC-Msp (lane 3). Molecular
    Figure Legend Snippet: Reactivities of Msp antisera with T. denticola ATCC 35405 outer membrane protein extracts. (Panel A) SDS-PAGE gel of outer membrane proteins. (Panel B) Western blots reacted with antisera to rN-Msp (lane 1), rV-Msp (lane 2), or rC-Msp (lane 3). Molecular

    Techniques Used: SDS Page, Western Blot

    Binding of rMsp to human fibronectin and to 30-kDa N-terminal fragment of human fibronectin. (Panel A) Western blot overlay of trypsin-derived fragments of human plasma fibronectin reacted with rMsp (lane 1) or with biotinylated T. denticola ATCC 35405
    Figure Legend Snippet: Binding of rMsp to human fibronectin and to 30-kDa N-terminal fragment of human fibronectin. (Panel A) Western blot overlay of trypsin-derived fragments of human plasma fibronectin reacted with rMsp (lane 1) or with biotinylated T. denticola ATCC 35405

    Techniques Used: Binding Assay, Western Blot, Derivative Assay

    Diagrammatic representation of the Msp sequences from T. denticola ATCC 35520 (A), strain ATCC 35405 (B), and of recombinant Msp polypeptides rMsp (530 aa residues), rN-Msp (189 aa residues), rV-Msp (57 aa residues), and rN-Msp (272 aa residues), with
    Figure Legend Snippet: Diagrammatic representation of the Msp sequences from T. denticola ATCC 35520 (A), strain ATCC 35405 (B), and of recombinant Msp polypeptides rMsp (530 aa residues), rN-Msp (189 aa residues), rV-Msp (57 aa residues), and rN-Msp (272 aa residues), with

    Techniques Used: Recombinant

    Effect of exogenously added rMsp on adhesion of Treponema strains to immobilized human fibronectin or 30-kDa fibronectin fragment. (Panel A) Adhesion levels of T. denticola ATCC 35405 cells to 0.1 μg fibronectin (filled column) or 30-kDa fibronectin
    Figure Legend Snippet: Effect of exogenously added rMsp on adhesion of Treponema strains to immobilized human fibronectin or 30-kDa fibronectin fragment. (Panel A) Adhesion levels of T. denticola ATCC 35405 cells to 0.1 μg fibronectin (filled column) or 30-kDa fibronectin

    Techniques Used:

    26) Product Images from "The opdB Locus Encodes the Trypsin-Like Peptidase Activity of Treponema denticola"

    Article Title: The opdB Locus Encodes the Trypsin-Like Peptidase Activity of Treponema denticola

    Journal: Infection and Immunity

    doi: 10.1128/IAI.69.10.6193-6200.2001

    SDS-PAGE analysis of T. denticola ATCC 35405 and opdB mutant BAE whole-cell extracts. Molecular mass standards are shown in the left lane. Arrow, band at approximately 78 kDa that is present in ATCC 35405 and that appears to be missing in BAE. This is consistent with the predicted molecular mass of the OpdB peptide.
    Figure Legend Snippet: SDS-PAGE analysis of T. denticola ATCC 35405 and opdB mutant BAE whole-cell extracts. Molecular mass standards are shown in the left lane. Arrow, band at approximately 78 kDa that is present in ATCC 35405 and that appears to be missing in BAE. This is consistent with the predicted molecular mass of the OpdB peptide.

    Techniques Used: SDS Page, Mutagenesis

    Confirmation of opdB mutant construction. (A) PCR amplification of opdB in T. denticola ATCC 35405 and isogenic opdB mutant BAE. Genomic DNAs were subjected to PCR using primers CX203 and CX204. (B) Southern blot analysis of T. denticola ATCC 35405 and isogenic opdB mutant BAE. Genomic DNAs were digested with Hin dIII and hybridized with a biotinylated internal fragment of opdB or the Sac I- Acc I fragment of ermF/AM . The ermF/AM cassette contains a single Hin dIII site.
    Figure Legend Snippet: Confirmation of opdB mutant construction. (A) PCR amplification of opdB in T. denticola ATCC 35405 and isogenic opdB mutant BAE. Genomic DNAs were subjected to PCR using primers CX203 and CX204. (B) Southern blot analysis of T. denticola ATCC 35405 and isogenic opdB mutant BAE. Genomic DNAs were digested with Hin dIII and hybridized with a biotinylated internal fragment of opdB or the Sac I- Acc I fragment of ermF/AM . The ermF/AM cassette contains a single Hin dIII site.

    Techniques Used: Mutagenesis, Polymerase Chain Reaction, Amplification, Southern Blot

    Growth of T. denticola ATCC 35405 and isogenic opdB mutant BAE. Bacteria were inoculated in NOS media and incubated under anaerobic conditions. A 600 was measured every 8 h for 5 days and every 24 h for the next 5 days. Error bars represent the range of A 600 values obtained from triplicate samples.
    Figure Legend Snippet: Growth of T. denticola ATCC 35405 and isogenic opdB mutant BAE. Bacteria were inoculated in NOS media and incubated under anaerobic conditions. A 600 was measured every 8 h for 5 days and every 24 h for the next 5 days. Error bars represent the range of A 600 values obtained from triplicate samples.

    Techniques Used: Mutagenesis, Incubation

    Enzymatic activities of T. denticola ATCC 35405 and opdB mutant BAE. (A) Trypsin-like activity measured by BA p NA hydrolysis. (B) Chymotrypsin-like activity measured by SAA p NA hydrolysis. NOS media, culture medium negative control. Vertical bars show standard deviations of triplicate samples. (C) API-ZYM strip. Tested enzymes: 1, control; 2, alkaline phosphatase; 3, esterase; 4, esterase lipase; 5, lipase; 6, leucine arylamidase; 7, valine arylamidase; 8, cystine arylamidase; 9, trypsin; 10, α-chymotrypsin; 11, acid phosphatase; 12, naphthol-AS-BI-phosphohydrolase; 13, α-galactosidase; 14, β-galactosidase; 15, β-glucuronidase; 16, α-glucosidase; 17, β-glucosidase; 18, N -acetyl-β-glucosaminidase; 19, α-mannosidase; 20, α-fucosidase. Arrow, substrate for the trypsin assay (BANA).
    Figure Legend Snippet: Enzymatic activities of T. denticola ATCC 35405 and opdB mutant BAE. (A) Trypsin-like activity measured by BA p NA hydrolysis. (B) Chymotrypsin-like activity measured by SAA p NA hydrolysis. NOS media, culture medium negative control. Vertical bars show standard deviations of triplicate samples. (C) API-ZYM strip. Tested enzymes: 1, control; 2, alkaline phosphatase; 3, esterase; 4, esterase lipase; 5, lipase; 6, leucine arylamidase; 7, valine arylamidase; 8, cystine arylamidase; 9, trypsin; 10, α-chymotrypsin; 11, acid phosphatase; 12, naphthol-AS-BI-phosphohydrolase; 13, α-galactosidase; 14, β-galactosidase; 15, β-glucuronidase; 16, α-glucosidase; 17, β-glucosidase; 18, N -acetyl-β-glucosaminidase; 19, α-mannosidase; 20, α-fucosidase. Arrow, substrate for the trypsin assay (BANA).

    Techniques Used: Mutagenesis, Activity Assay, Negative Control, Stripping Membranes

    27) Product Images from "Immunotopological Analysis of the Treponema denticola Major Surface Protein (Msp)"

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

    Journal: Journal of Bacteriology

    doi: 10.1128/JB.00528-18

    Immunofluorescence microscopy of T. denticola , revealing the Msp surface domain. T. denticola ATCC 35405 and ATCC 33520, grown to an OD 600 of 0.2, were fixed on glass slides with 1% paraformaldehyde, incubated with PBS or PBS plus 0.5% Triton X-100, and probed with rabbit antibodies to native ATCC 35405 Msp or recombinant FlaA, followed by goat anti-rabbit IgG conjugated to Alexa Fluor 568 (Msp) or Alexa Fluor 488 (FlaA), or with DAPI. Images were obtained at a magnification of 600× using an Olympus BX40 microscope fitted with an Olympus DP73 camera.
    Figure Legend Snippet: Immunofluorescence microscopy of T. denticola , revealing the Msp surface domain. T. denticola ATCC 35405 and ATCC 33520, grown to an OD 600 of 0.2, were fixed on glass slides with 1% paraformaldehyde, incubated with PBS or PBS plus 0.5% Triton X-100, and probed with rabbit antibodies to native ATCC 35405 Msp or recombinant FlaA, followed by goat anti-rabbit IgG conjugated to Alexa Fluor 568 (Msp) or Alexa Fluor 488 (FlaA), or with DAPI. Images were obtained at a magnification of 600× using an Olympus BX40 microscope fitted with an Olympus DP73 camera.

    Techniques Used: Immunofluorescence, Microscopy, Incubation, Recombinant

    Map and immunoblots of deletion mutations made in msp for expression in E. coli . (Upper) The 543-residue Msp protein, with the signal peptide (SP) cleavage site indicated (residue 20), is shown above the deletions made in the coding region. The amino acid residues deleted in the N-terminal region in each of the three constructs are indicated. Deletions in the central region within the approximate boundaries of the central domain (D1 through D2) include predicted antigenic domains (Ag1 and Ag2), the remaining region of greatest divergence between Msps of strains ATCC 35405 and ATCC 33520 (Xr), and D2. These mutant Msps were expressed in E. coli . (Lower) Immunoblots of E. coli strains expressing full-length Msps with the indicated Msp residues deleted are shown. T. denticola ATCC 35405 serves as a positive control. Blots were probed with rabbit polyclonal antibodies raised against native ATCC 35405 Msp, the Msp N-terminal domain, or whole T. denticola (Td) cells. All samples were boiled prior to electrophoresis. Lanes contain lysates of E. coli strains. Antibodies raised against native T. denticola ATCC 35405 Msp or whole T. denticola ATCC 35405 cells do not recognize recombinant Msps lacking residues 229 to 251.
    Figure Legend Snippet: Map and immunoblots of deletion mutations made in msp for expression in E. coli . (Upper) The 543-residue Msp protein, with the signal peptide (SP) cleavage site indicated (residue 20), is shown above the deletions made in the coding region. The amino acid residues deleted in the N-terminal region in each of the three constructs are indicated. Deletions in the central region within the approximate boundaries of the central domain (D1 through D2) include predicted antigenic domains (Ag1 and Ag2), the remaining region of greatest divergence between Msps of strains ATCC 35405 and ATCC 33520 (Xr), and D2. These mutant Msps were expressed in E. coli . (Lower) Immunoblots of E. coli strains expressing full-length Msps with the indicated Msp residues deleted are shown. T. denticola ATCC 35405 serves as a positive control. Blots were probed with rabbit polyclonal antibodies raised against native ATCC 35405 Msp, the Msp N-terminal domain, or whole T. denticola (Td) cells. All samples were boiled prior to electrophoresis. Lanes contain lysates of E. coli strains. Antibodies raised against native T. denticola ATCC 35405 Msp or whole T. denticola ATCC 35405 cells do not recognize recombinant Msps lacking residues 229 to 251.

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

    Models for T. denticola ATCC 35405 Msp generated by I-TASSER. The I-TASSER algorithm generates 5 predicted structural models based on several parameters, of which model 1 is the overall best model. Overall model ranking does not necessarily follow the C scores for proteins lacking closely related known structures. All 5 models are displayed to show the N termini (blue) and C termini (red). The ATCC 35405 Msp surface-exposed epitope (residues 229 to 251) is highlighted in green in each model. (A) Models 1 to 5 generated using the PDB data available in June 2017. (B) Models 1 to 5 generated using the PDB data available in October 2018.
    Figure Legend Snippet: Models for T. denticola ATCC 35405 Msp generated by I-TASSER. The I-TASSER algorithm generates 5 predicted structural models based on several parameters, of which model 1 is the overall best model. Overall model ranking does not necessarily follow the C scores for proteins lacking closely related known structures. All 5 models are displayed to show the N termini (blue) and C termini (red). The ATCC 35405 Msp surface-exposed epitope (residues 229 to 251) is highlighted in green in each model. (A) Models 1 to 5 generated using the PDB data available in June 2017. (B) Models 1 to 5 generated using the PDB data available in October 2018.

    Techniques Used: Generated

    28) Product Images from "Immunotopological Analysis of the Treponema denticola Major Surface Protein (Msp)"

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

    Journal: Journal of Bacteriology

    doi: 10.1128/JB.00528-18

    Immunofluorescence microscopy of T. denticola , revealing the Msp surface domain. T. denticola ATCC 35405 and ATCC 33520, grown to an OD 600 of 0.2, were fixed on glass slides with 1% paraformaldehyde, incubated with PBS or PBS plus 0.5% Triton X-100, and probed with rabbit antibodies to native ATCC 35405 Msp or recombinant FlaA, followed by goat anti-rabbit IgG conjugated to Alexa Fluor 568 (Msp) or Alexa Fluor 488 (FlaA), or with DAPI. Images were obtained at a magnification of 600× using an Olympus BX40 microscope fitted with an Olympus DP73 camera.
    Figure Legend Snippet: Immunofluorescence microscopy of T. denticola , revealing the Msp surface domain. T. denticola ATCC 35405 and ATCC 33520, grown to an OD 600 of 0.2, were fixed on glass slides with 1% paraformaldehyde, incubated with PBS or PBS plus 0.5% Triton X-100, and probed with rabbit antibodies to native ATCC 35405 Msp or recombinant FlaA, followed by goat anti-rabbit IgG conjugated to Alexa Fluor 568 (Msp) or Alexa Fluor 488 (FlaA), or with DAPI. Images were obtained at a magnification of 600× using an Olympus BX40 microscope fitted with an Olympus DP73 camera.

    Techniques Used: Immunofluorescence, Microscopy, Incubation, Recombinant

    Map and immunoblots of deletion mutations made in msp for expression in E. coli . (Upper) The 543-residue Msp protein, with the signal peptide (SP) cleavage site indicated (residue 20), is shown above the deletions made in the coding region. The amino acid residues deleted in the N-terminal region in each of the three constructs are indicated. Deletions in the central region within the approximate boundaries of the central domain (D1 through D2) include predicted antigenic domains (Ag1 and Ag2), the remaining region of greatest divergence between Msps of strains ATCC 35405 and ATCC 33520 (Xr), and D2. These mutant Msps were expressed in E. coli . (Lower) Immunoblots of E. coli strains expressing full-length Msps with the indicated Msp residues deleted are shown. T. denticola ATCC 35405 serves as a positive control. Blots were probed with rabbit polyclonal antibodies raised against native ATCC 35405 Msp, the Msp N-terminal domain, or whole T. denticola (Td) cells. All samples were boiled prior to electrophoresis. Lanes contain lysates of E. coli strains. Antibodies raised against native T. denticola ATCC 35405 Msp or whole T. denticola ATCC 35405 cells do not recognize recombinant Msps lacking residues 229 to 251.
    Figure Legend Snippet: Map and immunoblots of deletion mutations made in msp for expression in E. coli . (Upper) The 543-residue Msp protein, with the signal peptide (SP) cleavage site indicated (residue 20), is shown above the deletions made in the coding region. The amino acid residues deleted in the N-terminal region in each of the three constructs are indicated. Deletions in the central region within the approximate boundaries of the central domain (D1 through D2) include predicted antigenic domains (Ag1 and Ag2), the remaining region of greatest divergence between Msps of strains ATCC 35405 and ATCC 33520 (Xr), and D2. These mutant Msps were expressed in E. coli . (Lower) Immunoblots of E. coli strains expressing full-length Msps with the indicated Msp residues deleted are shown. T. denticola ATCC 35405 serves as a positive control. Blots were probed with rabbit polyclonal antibodies raised against native ATCC 35405 Msp, the Msp N-terminal domain, or whole T. denticola (Td) cells. All samples were boiled prior to electrophoresis. Lanes contain lysates of E. coli strains. Antibodies raised against native T. denticola ATCC 35405 Msp or whole T. denticola ATCC 35405 cells do not recognize recombinant Msps lacking residues 229 to 251.

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

    Models for T. denticola ATCC 35405 Msp generated by I-TASSER. The I-TASSER algorithm generates 5 predicted structural models based on several parameters, of which model 1 is the overall best model. Overall model ranking does not necessarily follow the C scores for proteins lacking closely related known structures. All 5 models are displayed to show the N termini (blue) and C termini (red). The ATCC 35405 Msp surface-exposed epitope (residues 229 to 251) is highlighted in green in each model. (A) Models 1 to 5 generated using the PDB data available in June 2017. (B) Models 1 to 5 generated using the PDB data available in October 2018.
    Figure Legend Snippet: Models for T. denticola ATCC 35405 Msp generated by I-TASSER. The I-TASSER algorithm generates 5 predicted structural models based on several parameters, of which model 1 is the overall best model. Overall model ranking does not necessarily follow the C scores for proteins lacking closely related known structures. All 5 models are displayed to show the N termini (blue) and C termini (red). The ATCC 35405 Msp surface-exposed epitope (residues 229 to 251) is highlighted in green in each model. (A) Models 1 to 5 generated using the PDB data available in June 2017. (B) Models 1 to 5 generated using the PDB data available in October 2018.

    Techniques Used: Generated

    29) Product Images from "The central region of the msp gene of Treponema denticola has sequence heterogeneity among clinical samples, obtained from patients with periodontitis"

    Article Title: The central region of the msp gene of Treponema denticola has sequence heterogeneity among clinical samples, obtained from patients with periodontitis

    Journal: BMC Infectious Diseases

    doi: 10.1186/1471-2334-10-345

    MSP amino acid sequence alignment of T. denticola strains ATCC 35405 and Group A (panel A), and ATCC 33520 and Group B (panel B) . The grey areas indicate single amino acid substitutions compared with ATCC 35405 (panel A) and ATCC 33520 (panel B).
    Figure Legend Snippet: MSP amino acid sequence alignment of T. denticola strains ATCC 35405 and Group A (panel A), and ATCC 33520 and Group B (panel B) . The grey areas indicate single amino acid substitutions compared with ATCC 35405 (panel A) and ATCC 33520 (panel B).

    Techniques Used: Sequencing

    Diversity of msp sequences . Sequence alignments of 17 central regions (from 600 to 900 nucleotides) from T. denticola positive clinical specimens. In panel A are shown the clinical samples of Group A. In panel B are shown the clinical samples of Group B. The upper line contains the sequence of T. denticola strain ATCC 35405 and ATCC 33520, respectively, in both panels. The grey areas indicate variations of single nucleotide positions compared with T. denticola ATCC 35405.
    Figure Legend Snippet: Diversity of msp sequences . Sequence alignments of 17 central regions (from 600 to 900 nucleotides) from T. denticola positive clinical specimens. In panel A are shown the clinical samples of Group A. In panel B are shown the clinical samples of Group B. The upper line contains the sequence of T. denticola strain ATCC 35405 and ATCC 33520, respectively, in both panels. The grey areas indicate variations of single nucleotide positions compared with T. denticola ATCC 35405.

    Techniques Used: Sequencing

    Evolutionary relationships of T. denticola msp gene, deduced from the sequences of 17 clinical samples, ATCC 35405, ATCC 33520, and OTK . The phylogenetic analysis was performed using the neighbor-joining method with MEGA 4 on aligned sequences from the msp complete cds sequence (bootstrap values > 75 are shown at nodes).
    Figure Legend Snippet: Evolutionary relationships of T. denticola msp gene, deduced from the sequences of 17 clinical samples, ATCC 35405, ATCC 33520, and OTK . The phylogenetic analysis was performed using the neighbor-joining method with MEGA 4 on aligned sequences from the msp complete cds sequence (bootstrap values > 75 are shown at nodes).

    Techniques Used: Sequencing

    Antigenicity plot of T. denticola strains ATCC 35405 (frame A), ATCC 33520 (frame B), and 2 representative specimens (B66, frame C; B23, frame D) . In each frame, the area of the plot that is surrounded by a continuous line represents the central region of MSP. The internal smaller area, surrounded by the dotted line, represents the portion that has the greatest difference in predicted antigenicity between specimens B66 and B23 and ATCC35405.
    Figure Legend Snippet: Antigenicity plot of T. denticola strains ATCC 35405 (frame A), ATCC 33520 (frame B), and 2 representative specimens (B66, frame C; B23, frame D) . In each frame, the area of the plot that is surrounded by a continuous line represents the central region of MSP. The internal smaller area, surrounded by the dotted line, represents the portion that has the greatest difference in predicted antigenicity between specimens B66 and B23 and ATCC35405.

    Techniques Used:

    30) Product Images from "The central region of the msp gene of Treponema denticola has sequence heterogeneity among clinical samples, obtained from patients with periodontitis"

    Article Title: The central region of the msp gene of Treponema denticola has sequence heterogeneity among clinical samples, obtained from patients with periodontitis

    Journal: BMC Infectious Diseases

    doi: 10.1186/1471-2334-10-345

    MSP amino acid sequence alignment of T. denticola strains ATCC 35405 and Group A (panel A), and ATCC 33520 and Group B (panel B) . The grey areas indicate single amino acid substitutions compared with ATCC 35405 (panel A) and ATCC 33520 (panel B).
    Figure Legend Snippet: MSP amino acid sequence alignment of T. denticola strains ATCC 35405 and Group A (panel A), and ATCC 33520 and Group B (panel B) . The grey areas indicate single amino acid substitutions compared with ATCC 35405 (panel A) and ATCC 33520 (panel B).

    Techniques Used: Sequencing

    Diversity of msp sequences . Sequence alignments of 17 central regions (from 600 to 900 nucleotides) from T. denticola positive clinical specimens. In panel A are shown the clinical samples of Group A. In panel B are shown the clinical samples of Group B. The upper line contains the sequence of T. denticola strain ATCC 35405 and ATCC 33520, respectively, in both panels. The grey areas indicate variations of single nucleotide positions compared with T. denticola ATCC 35405.
    Figure Legend Snippet: Diversity of msp sequences . Sequence alignments of 17 central regions (from 600 to 900 nucleotides) from T. denticola positive clinical specimens. In panel A are shown the clinical samples of Group A. In panel B are shown the clinical samples of Group B. The upper line contains the sequence of T. denticola strain ATCC 35405 and ATCC 33520, respectively, in both panels. The grey areas indicate variations of single nucleotide positions compared with T. denticola ATCC 35405.

    Techniques Used: Sequencing

    Evolutionary relationships of T. denticola msp gene, deduced from the sequences of 17 clinical samples, ATCC 35405, ATCC 33520, and OTK . The phylogenetic analysis was performed using the neighbor-joining method with MEGA 4 on aligned sequences from the msp complete cds sequence (bootstrap values > 75 are shown at nodes).
    Figure Legend Snippet: Evolutionary relationships of T. denticola msp gene, deduced from the sequences of 17 clinical samples, ATCC 35405, ATCC 33520, and OTK . The phylogenetic analysis was performed using the neighbor-joining method with MEGA 4 on aligned sequences from the msp complete cds sequence (bootstrap values > 75 are shown at nodes).

    Techniques Used: Sequencing

    Antigenicity plot of T. denticola strains ATCC 35405 (frame A), ATCC 33520 (frame B), and 2 representative specimens (B66, frame C; B23, frame D) . In each frame, the area of the plot that is surrounded by a continuous line represents the central region of MSP. The internal smaller area, surrounded by the dotted line, represents the portion that has the greatest difference in predicted antigenicity between specimens B66 and B23 and ATCC35405.
    Figure Legend Snippet: Antigenicity plot of T. denticola strains ATCC 35405 (frame A), ATCC 33520 (frame B), and 2 representative specimens (B66, frame C; B23, frame D) . In each frame, the area of the plot that is surrounded by a continuous line represents the central region of MSP. The internal smaller area, surrounded by the dotted line, represents the portion that has the greatest difference in predicted antigenicity between specimens B66 and B23 and ATCC35405.

    Techniques Used:

    31) Product Images from "Identification of a Treponema denticola OppA Homologue That Binds Host Proteins Present in the Subgingival Environment"

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

    Journal: Infection and Immunity

    doi:

    Binding of soluble host proteins to T. denticola cells and proteins. (A) ELISA format. FN, plasminogen (Pgn), or BSA in PBS were added to wells containing immobilized T. denticola ATCC 35405 cells (T.d.), native OppA (OppA), recombinant LacZ-OppA fusion protein (rOppA40), recombinant Msp (rMsp), or BSA. Bound FN and plasminogen were detected with anti-FN (shaded bars) and anti-plasminogen (hatched bars) antibodies, respectively. The y axis shows absorbance at 405 nm. Data shown represent the means ± standard deviations of at least two experiments using triplicate samples. (B) Ligand blot format. Duplicate samples of protein (1 μg) or cells (0.1 ml, OD 600 = 0.2) applied to nitrocellulose membranes were probed with plasminogen (samples 2 to 4) or plasminogen plus EACA (sample 5). Bound plasminogen was detected with anti-plasminogen immunoglobulin G. Lanes: 1, Plasminogen; 2, 5, and 6, T. denticola ATCC 35405; 3, T. denticola OHE; 4, T. denticola MHE.
    Figure Legend Snippet: Binding of soluble host proteins to T. denticola cells and proteins. (A) ELISA format. FN, plasminogen (Pgn), or BSA in PBS were added to wells containing immobilized T. denticola ATCC 35405 cells (T.d.), native OppA (OppA), recombinant LacZ-OppA fusion protein (rOppA40), recombinant Msp (rMsp), or BSA. Bound FN and plasminogen were detected with anti-FN (shaded bars) and anti-plasminogen (hatched bars) antibodies, respectively. The y axis shows absorbance at 405 nm. Data shown represent the means ± standard deviations of at least two experiments using triplicate samples. (B) Ligand blot format. Duplicate samples of protein (1 μg) or cells (0.1 ml, OD 600 = 0.2) applied to nitrocellulose membranes were probed with plasminogen (samples 2 to 4) or plasminogen plus EACA (sample 5). Bound plasminogen was detected with anti-plasminogen immunoglobulin G. Lanes: 1, Plasminogen; 2, 5, and 6, T. denticola ATCC 35405; 3, T. denticola OHE; 4, T. denticola MHE.

    Techniques Used: Binding Assay, Enzyme-linked Immunosorbent Assay, Recombinant

    Confirmation of construction of allelic replacement mutants in the opp locus. (A) Southern blots of Sca I-digested T. denticola genomic DNA were probed with a biotinylated internal oppA fragment ( opp ) and the 2.1-kb ermF/AM cassette ( erm ). The ermF/AM cassette contains a single Sca I site. (B) Western immunoblot of T. denticola lysates probed with anti-70 antibodies. Lanes: 1, parent strain ATCC 35405; 2, oppA mutant strain OHE; 3, oppF mutant strain OXE.
    Figure Legend Snippet: Confirmation of construction of allelic replacement mutants in the opp locus. (A) Southern blots of Sca I-digested T. denticola genomic DNA were probed with a biotinylated internal oppA fragment ( opp ) and the 2.1-kb ermF/AM cassette ( erm ). The ermF/AM cassette contains a single Sca I site. (B) Western immunoblot of T. denticola lysates probed with anti-70 antibodies. Lanes: 1, parent strain ATCC 35405; 2, oppA mutant strain OHE; 3, oppF mutant strain OXE.

    Techniques Used: Western Blot, Mutagenesis

    Conservation of oppA in oral Treponema strains. (A) Southern blot of Hin dIII-digested chromosomal DNA probed with a 0.9-kb internal fragment of oppA . (B) Western blot of whole-cell extracts probed with anti-40 antibodies. Lanes: 1, T. denticola ATCC 35405; 2, T. denticola ATCC 35404; 3, T. denticola ATCC 33520; 4, T. vincentii LA-1; 5, T. denticola OTK; 6, T. denticola GM-1; 7, T. socranskii ATCC 35536; 8, T. pectinovorum ATCC 33768.
    Figure Legend Snippet: Conservation of oppA in oral Treponema strains. (A) Southern blot of Hin dIII-digested chromosomal DNA probed with a 0.9-kb internal fragment of oppA . (B) Western blot of whole-cell extracts probed with anti-40 antibodies. Lanes: 1, T. denticola ATCC 35405; 2, T. denticola ATCC 35404; 3, T. denticola ATCC 33520; 4, T. vincentii LA-1; 5, T. denticola OTK; 6, T. denticola GM-1; 7, T. socranskii ATCC 35536; 8, T. pectinovorum ATCC 33768.

    Techniques Used: Southern Blot, Western Blot

    32) Product Images from "Dentipain, a Streptococcus-pyogenes-IdeS-protease homologue, is a novel virulence factor of Treponema denticola"

    Article Title: Dentipain, a Streptococcus-pyogenes-IdeS-protease homologue, is a novel virulence factor of Treponema denticola

    Journal: Biological chemistry

    doi: 10.1515/BC.2010.113

    Construction of an IdeT protease-deficient mutant A . (i) The wild-type ideT locus detailing the four protein domains; (ii) pIDEKO4, constructed using pMCL191, two ideT PCR generated fragments flanking the proteolytic domain (hatched bar and dotted bar) and an erythromycin resistance cassette derived from pVA2198. The restriction sites introduced during PCR are also shown; (iii) the ideT mutant locus detailing the dentipain region replaced with an erythromycin resistance cassette by homologous recombination. B . (i) PCR amplification of the ideT locus using primers ID-1 and ID-4, which amplify from amino acid residues 172 to 640. Lane 1, T. denticola ATCC 35405; lane 2, T. denticola IDEKO4; lane 3, T. denticola Ide5; lane 4, T. denticola Ide6; lane 5 , Molecular size marker. (ii) PCR amplification of the ideT locus using primers ID-1 and CATU, which amplify from amino acid residues 172 to 417. Lane 1, T. denticola ATCC 35405; lane 2, T. denticola IDEKO4; lane 3 , Molecular size marker.
    Figure Legend Snippet: Construction of an IdeT protease-deficient mutant A . (i) The wild-type ideT locus detailing the four protein domains; (ii) pIDEKO4, constructed using pMCL191, two ideT PCR generated fragments flanking the proteolytic domain (hatched bar and dotted bar) and an erythromycin resistance cassette derived from pVA2198. The restriction sites introduced during PCR are also shown; (iii) the ideT mutant locus detailing the dentipain region replaced with an erythromycin resistance cassette by homologous recombination. B . (i) PCR amplification of the ideT locus using primers ID-1 and ID-4, which amplify from amino acid residues 172 to 640. Lane 1, T. denticola ATCC 35405; lane 2, T. denticola IDEKO4; lane 3, T. denticola Ide5; lane 4, T. denticola Ide6; lane 5 , Molecular size marker. (ii) PCR amplification of the ideT locus using primers ID-1 and CATU, which amplify from amino acid residues 172 to 417. Lane 1, T. denticola ATCC 35405; lane 2, T. denticola IDEKO4; lane 3 , Molecular size marker.

    Techniques Used: Mutagenesis, Construct, Polymerase Chain Reaction, Generated, Derivative Assay, Homologous Recombination, Amplification, Marker

    Analysis of IdeT translation A. SDS-PAGE of T. denticola sonicates. Lane 1, T. denticola ATCC 35405 sonicate; lane 2, T. denticola IDEKO4 sonicate. B. Immunoblot analysis of IdeT from T. denticola cells. Lane 1, T. denticola ATCC 35405 sonicate; lane 2, T. denticola IDEKO4 sonicate. Antibody: rabbit serum anti-IdeT recombinant protein (219–647). The arrow indicates the band which reacted with this antibody. C. SDS-PAGE of concentrated culture supernatant of T. denticola . Culture supernatant of T. denticola grown in E-TYGV medium was collected and concentrated. Lane 1, culture supernatant of T. denticola ATCC 35405; lane 2, culture supernatant of T. denticola IDEKO4. D. Immunoblot analysis of IdeT in culture supernatants. Lane 1, culture supernatant of T. denticola ATCC 35405; lane 2, culture supernatant of T. denticola IDEKO4. Antibody: rabbit serum anti-IdeT recombinant protein (219–647). The arrow indicates the band which reacted with this antibody. E. Immunoblot analysis of IdeT in culture supernatants. Lane 1, culture supernatant of T. denticola ATCC 3540 5; lane 2, culture supernatant of T. denticola IDEK O4. Antibody : rabbit serum anti-IdeT synthetic peptide (IdeT498–511). The arrow indicates the band which reacted with this antibody.
    Figure Legend Snippet: Analysis of IdeT translation A. SDS-PAGE of T. denticola sonicates. Lane 1, T. denticola ATCC 35405 sonicate; lane 2, T. denticola IDEKO4 sonicate. B. Immunoblot analysis of IdeT from T. denticola cells. Lane 1, T. denticola ATCC 35405 sonicate; lane 2, T. denticola IDEKO4 sonicate. Antibody: rabbit serum anti-IdeT recombinant protein (219–647). The arrow indicates the band which reacted with this antibody. C. SDS-PAGE of concentrated culture supernatant of T. denticola . Culture supernatant of T. denticola grown in E-TYGV medium was collected and concentrated. Lane 1, culture supernatant of T. denticola ATCC 35405; lane 2, culture supernatant of T. denticola IDEKO4. D. Immunoblot analysis of IdeT in culture supernatants. Lane 1, culture supernatant of T. denticola ATCC 35405; lane 2, culture supernatant of T. denticola IDEKO4. Antibody: rabbit serum anti-IdeT recombinant protein (219–647). The arrow indicates the band which reacted with this antibody. E. Immunoblot analysis of IdeT in culture supernatants. Lane 1, culture supernatant of T. denticola ATCC 3540 5; lane 2, culture supernatant of T. denticola IDEK O4. Antibody : rabbit serum anti-IdeT synthetic peptide (IdeT498–511). The arrow indicates the band which reacted with this antibody.

    Techniques Used: SDS Page, Recombinant

    Analysis of the role of IdeT proteolytic activity in the virulence of T. denticola . Bars represent the mean area of lesions at the infection sites following challenge with either T. denticola ATCC 35405 or T. denticola IDEKO4. Mice were injected with live T. denticola ATCC 35405 (black bars) or IDEKO4 (open bars), and lesion areas determined at the indicated times following infection. Bars indicate standard deviation. *P
    Figure Legend Snippet: Analysis of the role of IdeT proteolytic activity in the virulence of T. denticola . Bars represent the mean area of lesions at the infection sites following challenge with either T. denticola ATCC 35405 or T. denticola IDEKO4. Mice were injected with live T. denticola ATCC 35405 (black bars) or IDEKO4 (open bars), and lesion areas determined at the indicated times following infection. Bars indicate standard deviation. *P

    Techniques Used: Activity Assay, Infection, Mouse Assay, Injection, Standard Deviation

    33) Product Images from "Dentipain, a Streptococcus-pyogenes-IdeS-protease homologue, is a novel virulence factor of Treponema denticola"

    Article Title: Dentipain, a Streptococcus-pyogenes-IdeS-protease homologue, is a novel virulence factor of Treponema denticola

    Journal: Biological chemistry

    doi: 10.1515/BC.2010.113

    Construction of an IdeT protease-deficient mutant A . (i) The wild-type ideT locus detailing the four protein domains; (ii) pIDEKO4, constructed using pMCL191, two ideT PCR generated fragments flanking the proteolytic domain (hatched bar and dotted bar) and an erythromycin resistance cassette derived from pVA2198. The restriction sites introduced during PCR are also shown; (iii) the ideT mutant locus detailing the dentipain region replaced with an erythromycin resistance cassette by homologous recombination. B . (i) PCR amplification of the ideT locus using primers ID-1 and ID-4, which amplify from amino acid residues 172 to 640. Lane 1, T. denticola ATCC 35405; lane 2, T. denticola IDEKO4; lane 3, T. denticola Ide5; lane 4, T. denticola Ide6; lane 5 , Molecular size marker. (ii) PCR amplification of the ideT locus using primers ID-1 and CATU, which amplify from amino acid residues 172 to 417. Lane 1, T. denticola ATCC 35405; lane 2, T. denticola IDEKO4; lane 3 , Molecular size marker.
    Figure Legend Snippet: Construction of an IdeT protease-deficient mutant A . (i) The wild-type ideT locus detailing the four protein domains; (ii) pIDEKO4, constructed using pMCL191, two ideT PCR generated fragments flanking the proteolytic domain (hatched bar and dotted bar) and an erythromycin resistance cassette derived from pVA2198. The restriction sites introduced during PCR are also shown; (iii) the ideT mutant locus detailing the dentipain region replaced with an erythromycin resistance cassette by homologous recombination. B . (i) PCR amplification of the ideT locus using primers ID-1 and ID-4, which amplify from amino acid residues 172 to 640. Lane 1, T. denticola ATCC 35405; lane 2, T. denticola IDEKO4; lane 3, T. denticola Ide5; lane 4, T. denticola Ide6; lane 5 , Molecular size marker. (ii) PCR amplification of the ideT locus using primers ID-1 and CATU, which amplify from amino acid residues 172 to 417. Lane 1, T. denticola ATCC 35405; lane 2, T. denticola IDEKO4; lane 3 , Molecular size marker.

    Techniques Used: Mutagenesis, Construct, Polymerase Chain Reaction, Generated, Derivative Assay, Homologous Recombination, Amplification, Marker

    Analysis of IdeT translation A. SDS-PAGE of T. denticola sonicates. Lane 1, T. denticola ATCC 35405 sonicate; lane 2, T. denticola IDEKO4 sonicate. B. Immunoblot analysis of IdeT from T. denticola cells. Lane 1, T. denticola ATCC 35405 sonicate; lane 2, T. denticola IDEKO4 sonicate. Antibody: rabbit serum anti-IdeT recombinant protein (219–647). The arrow indicates the band which reacted with this antibody. C. SDS-PAGE of concentrated culture supernatant of T. denticola . Culture supernatant of T. denticola grown in E-TYGV medium was collected and concentrated. Lane 1, culture supernatant of T. denticola ATCC 35405; lane 2, culture supernatant of T. denticola IDEKO4. D. Immunoblot analysis of IdeT in culture supernatants. Lane 1, culture supernatant of T. denticola ATCC 35405; lane 2, culture supernatant of T. denticola IDEKO4. Antibody: rabbit serum anti-IdeT recombinant protein (219–647). The arrow indicates the band which reacted with this antibody. E. Immunoblot analysis of IdeT in culture supernatants. Lane 1, culture supernatant of T. denticola ATCC 3540 5; lane 2, culture supernatant of T. denticola IDEK O4. Antibody : rabbit serum anti-IdeT synthetic peptide (IdeT498–511). The arrow indicates the band which reacted with this antibody.
    Figure Legend Snippet: Analysis of IdeT translation A. SDS-PAGE of T. denticola sonicates. Lane 1, T. denticola ATCC 35405 sonicate; lane 2, T. denticola IDEKO4 sonicate. B. Immunoblot analysis of IdeT from T. denticola cells. Lane 1, T. denticola ATCC 35405 sonicate; lane 2, T. denticola IDEKO4 sonicate. Antibody: rabbit serum anti-IdeT recombinant protein (219–647). The arrow indicates the band which reacted with this antibody. C. SDS-PAGE of concentrated culture supernatant of T. denticola . Culture supernatant of T. denticola grown in E-TYGV medium was collected and concentrated. Lane 1, culture supernatant of T. denticola ATCC 35405; lane 2, culture supernatant of T. denticola IDEKO4. D. Immunoblot analysis of IdeT in culture supernatants. Lane 1, culture supernatant of T. denticola ATCC 35405; lane 2, culture supernatant of T. denticola IDEKO4. Antibody: rabbit serum anti-IdeT recombinant protein (219–647). The arrow indicates the band which reacted with this antibody. E. Immunoblot analysis of IdeT in culture supernatants. Lane 1, culture supernatant of T. denticola ATCC 3540 5; lane 2, culture supernatant of T. denticola IDEK O4. Antibody : rabbit serum anti-IdeT synthetic peptide (IdeT498–511). The arrow indicates the band which reacted with this antibody.

    Techniques Used: SDS Page, Recombinant

    Analysis of the role of IdeT proteolytic activity in the virulence of T. denticola . Bars represent the mean area of lesions at the infection sites following challenge with either T. denticola ATCC 35405 or T. denticola IDEKO4. Mice were injected with live T. denticola ATCC 35405 (black bars) or IDEKO4 (open bars), and lesion areas determined at the indicated times following infection. Bars indicate standard deviation. *P
    Figure Legend Snippet: Analysis of the role of IdeT proteolytic activity in the virulence of T. denticola . Bars represent the mean area of lesions at the infection sites following challenge with either T. denticola ATCC 35405 or T. denticola IDEKO4. Mice were injected with live T. denticola ATCC 35405 (black bars) or IDEKO4 (open bars), and lesion areas determined at the indicated times following infection. Bars indicate standard deviation. *P

    Techniques Used: Activity Assay, Infection, Mouse Assay, Injection, Standard Deviation

    34) Product Images from "Dentipain, a Streptococcus-pyogenes-IdeS-protease homologue, is a novel virulence factor of Treponema denticola"

    Article Title: Dentipain, a Streptococcus-pyogenes-IdeS-protease homologue, is a novel virulence factor of Treponema denticola

    Journal: Biological chemistry

    doi: 10.1515/BC.2010.113

    Construction of an IdeT protease-deficient mutant A . (i) The wild-type ideT locus detailing the four protein domains; (ii) pIDEKO4, constructed using pMCL191, two ideT PCR generated fragments flanking the proteolytic domain (hatched bar and dotted bar) and an erythromycin resistance cassette derived from pVA2198. The restriction sites introduced during PCR are also shown; (iii) the ideT mutant locus detailing the dentipain region replaced with an erythromycin resistance cassette by homologous recombination. B . (i) PCR amplification of the ideT locus using primers ID-1 and ID-4, which amplify from amino acid residues 172 to 640. Lane 1, T. denticola ATCC 35405; lane 2, T. denticola IDEKO4; lane 3, T. denticola Ide5; lane 4, T. denticola Ide6; lane 5 , Molecular size marker. (ii) PCR amplification of the ideT locus using primers ID-1 and CATU, which amplify from amino acid residues 172 to 417. Lane 1, T. denticola ATCC 35405; lane 2, T. denticola IDEKO4; lane 3 , Molecular size marker.
    Figure Legend Snippet: Construction of an IdeT protease-deficient mutant A . (i) The wild-type ideT locus detailing the four protein domains; (ii) pIDEKO4, constructed using pMCL191, two ideT PCR generated fragments flanking the proteolytic domain (hatched bar and dotted bar) and an erythromycin resistance cassette derived from pVA2198. The restriction sites introduced during PCR are also shown; (iii) the ideT mutant locus detailing the dentipain region replaced with an erythromycin resistance cassette by homologous recombination. B . (i) PCR amplification of the ideT locus using primers ID-1 and ID-4, which amplify from amino acid residues 172 to 640. Lane 1, T. denticola ATCC 35405; lane 2, T. denticola IDEKO4; lane 3, T. denticola Ide5; lane 4, T. denticola Ide6; lane 5 , Molecular size marker. (ii) PCR amplification of the ideT locus using primers ID-1 and CATU, which amplify from amino acid residues 172 to 417. Lane 1, T. denticola ATCC 35405; lane 2, T. denticola IDEKO4; lane 3 , Molecular size marker.

    Techniques Used: Mutagenesis, Construct, Polymerase Chain Reaction, Generated, Derivative Assay, Homologous Recombination, Amplification, Marker

    Analysis of IdeT translation A. SDS-PAGE of T. denticola sonicates. Lane 1, T. denticola ATCC 35405 sonicate; lane 2, T. denticola IDEKO4 sonicate. B. Immunoblot analysis of IdeT from T. denticola cells. Lane 1, T. denticola ATCC 35405 sonicate; lane 2, T. denticola IDEKO4 sonicate. Antibody: rabbit serum anti-IdeT recombinant protein (219–647). The arrow indicates the band which reacted with this antibody. C. SDS-PAGE of concentrated culture supernatant of T. denticola . Culture supernatant of T. denticola grown in E-TYGV medium was collected and concentrated. Lane 1, culture supernatant of T. denticola ATCC 35405; lane 2, culture supernatant of T. denticola IDEKO4. D. Immunoblot analysis of IdeT in culture supernatants. Lane 1, culture supernatant of T. denticola ATCC 35405; lane 2, culture supernatant of T. denticola IDEKO4. Antibody: rabbit serum anti-IdeT recombinant protein (219–647). The arrow indicates the band which reacted with this antibody. E. Immunoblot analysis of IdeT in culture supernatants. Lane 1, culture supernatant of T. denticola ATCC 3540 5; lane 2, culture supernatant of T. denticola IDEK O4. Antibody : rabbit serum anti-IdeT synthetic peptide (IdeT498–511). The arrow indicates the band which reacted with this antibody.
    Figure Legend Snippet: Analysis of IdeT translation A. SDS-PAGE of T. denticola sonicates. Lane 1, T. denticola ATCC 35405 sonicate; lane 2, T. denticola IDEKO4 sonicate. B. Immunoblot analysis of IdeT from T. denticola cells. Lane 1, T. denticola ATCC 35405 sonicate; lane 2, T. denticola IDEKO4 sonicate. Antibody: rabbit serum anti-IdeT recombinant protein (219–647). The arrow indicates the band which reacted with this antibody. C. SDS-PAGE of concentrated culture supernatant of T. denticola . Culture supernatant of T. denticola grown in E-TYGV medium was collected and concentrated. Lane 1, culture supernatant of T. denticola ATCC 35405; lane 2, culture supernatant of T. denticola IDEKO4. D. Immunoblot analysis of IdeT in culture supernatants. Lane 1, culture supernatant of T. denticola ATCC 35405; lane 2, culture supernatant of T. denticola IDEKO4. Antibody: rabbit serum anti-IdeT recombinant protein (219–647). The arrow indicates the band which reacted with this antibody. E. Immunoblot analysis of IdeT in culture supernatants. Lane 1, culture supernatant of T. denticola ATCC 3540 5; lane 2, culture supernatant of T. denticola IDEK O4. Antibody : rabbit serum anti-IdeT synthetic peptide (IdeT498–511). The arrow indicates the band which reacted with this antibody.

    Techniques Used: SDS Page, Recombinant

    Analysis of the role of IdeT proteolytic activity in the virulence of T. denticola . Bars represent the mean area of lesions at the infection sites following challenge with either T. denticola ATCC 35405 or T. denticola IDEKO4. Mice were injected with live T. denticola ATCC 35405 (black bars) or IDEKO4 (open bars), and lesion areas determined at the indicated times following infection. Bars indicate standard deviation. *P
    Figure Legend Snippet: Analysis of the role of IdeT proteolytic activity in the virulence of T. denticola . Bars represent the mean area of lesions at the infection sites following challenge with either T. denticola ATCC 35405 or T. denticola IDEKO4. Mice were injected with live T. denticola ATCC 35405 (black bars) or IDEKO4 (open bars), and lesion areas determined at the indicated times following infection. Bars indicate standard deviation. *P

    Techniques Used: Activity Assay, Infection, Mouse Assay, Injection, Standard Deviation

    35) Product Images from "Dentipain, a Streptococcus-pyogenes-IdeS-protease homologue, is a novel virulence factor of Treponema denticola"

    Article Title: Dentipain, a Streptococcus-pyogenes-IdeS-protease homologue, is a novel virulence factor of Treponema denticola

    Journal: Biological chemistry

    doi: 10.1515/BC.2010.113

    Construction of an IdeT protease-deficient mutant A . (i) The wild-type ideT locus detailing the four protein domains; (ii) pIDEKO4, constructed using pMCL191, two ideT PCR generated fragments flanking the proteolytic domain (hatched bar and dotted bar) and an erythromycin resistance cassette derived from pVA2198. The restriction sites introduced during PCR are also shown; (iii) the ideT mutant locus detailing the dentipain region replaced with an erythromycin resistance cassette by homologous recombination. B . (i) PCR amplification of the ideT locus using primers ID-1 and ID-4, which amplify from amino acid residues 172 to 640. Lane 1, T. denticola ATCC 35405; lane 2, T. denticola IDEKO4; lane 3, T. denticola Ide5; lane 4, T. denticola Ide6; lane 5 , Molecular size marker. (ii) PCR amplification of the ideT locus using primers ID-1 and CATU, which amplify from amino acid residues 172 to 417. Lane 1, T. denticola ATCC 35405; lane 2, T. denticola IDEKO4; lane 3 , Molecular size marker.
    Figure Legend Snippet: Construction of an IdeT protease-deficient mutant A . (i) The wild-type ideT locus detailing the four protein domains; (ii) pIDEKO4, constructed using pMCL191, two ideT PCR generated fragments flanking the proteolytic domain (hatched bar and dotted bar) and an erythromycin resistance cassette derived from pVA2198. The restriction sites introduced during PCR are also shown; (iii) the ideT mutant locus detailing the dentipain region replaced with an erythromycin resistance cassette by homologous recombination. B . (i) PCR amplification of the ideT locus using primers ID-1 and ID-4, which amplify from amino acid residues 172 to 640. Lane 1, T. denticola ATCC 35405; lane 2, T. denticola IDEKO4; lane 3, T. denticola Ide5; lane 4, T. denticola Ide6; lane 5 , Molecular size marker. (ii) PCR amplification of the ideT locus using primers ID-1 and CATU, which amplify from amino acid residues 172 to 417. Lane 1, T. denticola ATCC 35405; lane 2, T. denticola IDEKO4; lane 3 , Molecular size marker.

    Techniques Used: Mutagenesis, Construct, Polymerase Chain Reaction, Generated, Derivative Assay, Homologous Recombination, Amplification, Marker

    Analysis of IdeT translation A. SDS-PAGE of T. denticola sonicates. Lane 1, T. denticola ATCC 35405 sonicate; lane 2, T. denticola IDEKO4 sonicate. B. Immunoblot analysis of IdeT from T. denticola cells. Lane 1, T. denticola ATCC 35405 sonicate; lane 2, T. denticola IDEKO4 sonicate. Antibody: rabbit serum anti-IdeT recombinant protein (219–647). The arrow indicates the band which reacted with this antibody. C. SDS-PAGE of concentrated culture supernatant of T. denticola . Culture supernatant of T. denticola grown in E-TYGV medium was collected and concentrated. Lane 1, culture supernatant of T. denticola ATCC 35405; lane 2, culture supernatant of T. denticola IDEKO4. D. Immunoblot analysis of IdeT in culture supernatants. Lane 1, culture supernatant of T. denticola ATCC 35405; lane 2, culture supernatant of T. denticola IDEKO4. Antibody: rabbit serum anti-IdeT recombinant protein (219–647). The arrow indicates the band which reacted with this antibody. E. Immunoblot analysis of IdeT in culture supernatants. Lane 1, culture supernatant of T. denticola ATCC 3540 5; lane 2, culture supernatant of T. denticola IDEK O4. Antibody : rabbit serum anti-IdeT synthetic peptide (IdeT498–511). The arrow indicates the band which reacted with this antibody.
    Figure Legend Snippet: Analysis of IdeT translation A. SDS-PAGE of T. denticola sonicates. Lane 1, T. denticola ATCC 35405 sonicate; lane 2, T. denticola IDEKO4 sonicate. B. Immunoblot analysis of IdeT from T. denticola cells. Lane 1, T. denticola ATCC 35405 sonicate; lane 2, T. denticola IDEKO4 sonicate. Antibody: rabbit serum anti-IdeT recombinant protein (219–647). The arrow indicates the band which reacted with this antibody. C. SDS-PAGE of concentrated culture supernatant of T. denticola . Culture supernatant of T. denticola grown in E-TYGV medium was collected and concentrated. Lane 1, culture supernatant of T. denticola ATCC 35405; lane 2, culture supernatant of T. denticola IDEKO4. D. Immunoblot analysis of IdeT in culture supernatants. Lane 1, culture supernatant of T. denticola ATCC 35405; lane 2, culture supernatant of T. denticola IDEKO4. Antibody: rabbit serum anti-IdeT recombinant protein (219–647). The arrow indicates the band which reacted with this antibody. E. Immunoblot analysis of IdeT in culture supernatants. Lane 1, culture supernatant of T. denticola ATCC 3540 5; lane 2, culture supernatant of T. denticola IDEK O4. Antibody : rabbit serum anti-IdeT synthetic peptide (IdeT498–511). The arrow indicates the band which reacted with this antibody.

    Techniques Used: SDS Page, Recombinant

    Analysis of the role of IdeT proteolytic activity in the virulence of T. denticola . Bars represent the mean area of lesions at the infection sites following challenge with either T. denticola ATCC 35405 or T. denticola IDEKO4. Mice were injected with live T. denticola ATCC 35405 (black bars) or IDEKO4 (open bars), and lesion areas determined at the indicated times following infection. Bars indicate standard deviation. *P
    Figure Legend Snippet: Analysis of the role of IdeT proteolytic activity in the virulence of T. denticola . Bars represent the mean area of lesions at the infection sites following challenge with either T. denticola ATCC 35405 or T. denticola IDEKO4. Mice were injected with live T. denticola ATCC 35405 (black bars) or IDEKO4 (open bars), and lesion areas determined at the indicated times following infection. Bars indicate standard deviation. *P

    Techniques Used: Activity Assay, Infection, Mouse Assay, Injection, Standard Deviation

    36) Product Images from "Identification of a Treponema denticola OppA Homologue That Binds Host Proteins Present in the Subgingival Environment"

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

    Journal: Infection and Immunity

    doi:

    Binding of soluble host proteins to T. denticola cells and proteins. (A) ELISA format. FN, plasminogen (Pgn), or BSA in PBS were added to wells containing immobilized T. denticola ATCC 35405 cells (T.d.), native OppA (OppA), recombinant LacZ-OppA fusion protein (rOppA40), recombinant Msp (rMsp), or BSA. Bound FN and plasminogen were detected with anti-FN (shaded bars) and anti-plasminogen (hatched bars) antibodies, respectively. The y axis shows absorbance at 405 nm. Data shown represent the means ± standard deviations of at least two experiments using triplicate samples. (B) Ligand blot format. Duplicate samples of protein (1 μg) or cells (0.1 ml, OD 600 = 0.2) applied to nitrocellulose membranes were probed with plasminogen (samples 2 to 4) or plasminogen plus EACA (sample 5). Bound plasminogen was detected with anti-plasminogen immunoglobulin G. Lanes: 1, Plasminogen; 2, 5, and 6, T. denticola ATCC 35405; 3, T. denticola OHE; 4, T. denticola MHE.
    Figure Legend Snippet: Binding of soluble host proteins to T. denticola cells and proteins. (A) ELISA format. FN, plasminogen (Pgn), or BSA in PBS were added to wells containing immobilized T. denticola ATCC 35405 cells (T.d.), native OppA (OppA), recombinant LacZ-OppA fusion protein (rOppA40), recombinant Msp (rMsp), or BSA. Bound FN and plasminogen were detected with anti-FN (shaded bars) and anti-plasminogen (hatched bars) antibodies, respectively. The y axis shows absorbance at 405 nm. Data shown represent the means ± standard deviations of at least two experiments using triplicate samples. (B) Ligand blot format. Duplicate samples of protein (1 μg) or cells (0.1 ml, OD 600 = 0.2) applied to nitrocellulose membranes were probed with plasminogen (samples 2 to 4) or plasminogen plus EACA (sample 5). Bound plasminogen was detected with anti-plasminogen immunoglobulin G. Lanes: 1, Plasminogen; 2, 5, and 6, T. denticola ATCC 35405; 3, T. denticola OHE; 4, T. denticola MHE.

    Techniques Used: Binding Assay, Enzyme-linked Immunosorbent Assay, Recombinant

    Confirmation of construction of allelic replacement mutants in the opp locus. (A) Southern blots of Sca I-digested T. denticola genomic DNA were probed with a biotinylated internal oppA fragment ( opp ) and the 2.1-kb ermF/AM cassette ( erm ). The ermF/AM cassette contains a single Sca I site. (B) Western immunoblot of T. denticola lysates probed with anti-70 antibodies. Lanes: 1, parent strain ATCC 35405; 2, oppA mutant strain OHE; 3, oppF mutant strain OXE.
    Figure Legend Snippet: Confirmation of construction of allelic replacement mutants in the opp locus. (A) Southern blots of Sca I-digested T. denticola genomic DNA were probed with a biotinylated internal oppA fragment ( opp ) and the 2.1-kb ermF/AM cassette ( erm ). The ermF/AM cassette contains a single Sca I site. (B) Western immunoblot of T. denticola lysates probed with anti-70 antibodies. Lanes: 1, parent strain ATCC 35405; 2, oppA mutant strain OHE; 3, oppF mutant strain OXE.

    Techniques Used: Western Blot, Mutagenesis

    Conservation of oppA in oral Treponema strains. (A) Southern blot of Hin dIII-digested chromosomal DNA probed with a 0.9-kb internal fragment of oppA . (B) Western blot of whole-cell extracts probed with anti-40 antibodies. Lanes: 1, T. denticola ATCC 35405; 2, T. denticola ATCC 35404; 3, T. denticola ATCC 33520; 4, T. vincentii LA-1; 5, T. denticola OTK; 6, T. denticola GM-1; 7, T. socranskii ATCC 35536; 8, T. pectinovorum ATCC 33768.
    Figure Legend Snippet: Conservation of oppA in oral Treponema strains. (A) Southern blot of Hin dIII-digested chromosomal DNA probed with a 0.9-kb internal fragment of oppA . (B) Western blot of whole-cell extracts probed with anti-40 antibodies. Lanes: 1, T. denticola ATCC 35405; 2, T. denticola ATCC 35404; 3, T. denticola ATCC 33520; 4, T. vincentii LA-1; 5, T. denticola OTK; 6, T. denticola GM-1; 7, T. socranskii ATCC 35536; 8, T. pectinovorum ATCC 33768.

    Techniques Used: Southern Blot, Western Blot

    37) Product Images from "Treponema denticola chymotrypsin-like proteinase (CTLP) integrates spirochaetes within oral microbial communities"

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

    Journal: Microbiology

    doi: 10.1099/mic.0.055939-0

    Role of the CTLP complex in the formation of T. denticola / P. gingivalis dual-species biofilms. Representative CLSM images of dual-species biofilms of (a, b) T. denticola ATCC 35405 and (c, d) T. denticola CKE, with P. gingivalis ATCC 33277. Biofilms were
    Figure Legend Snippet: Role of the CTLP complex in the formation of T. denticola / P. gingivalis dual-species biofilms. Representative CLSM images of dual-species biofilms of (a, b) T. denticola ATCC 35405 and (c, d) T. denticola CKE, with P. gingivalis ATCC 33277. Biofilms were

    Techniques Used: Confocal Laser Scanning Microscopy

    Adherence levels of Treponema to other periodontopathogens. The input cell number was 1.2×10 7 cells per well of T. denticola ATCC 35405 (black bars), T. denticola MHE (mid-grey bars), T. denticola CKE (dark-grey bars) and T. vincentii ATCC 35580
    Figure Legend Snippet: Adherence levels of Treponema to other periodontopathogens. The input cell number was 1.2×10 7 cells per well of T. denticola ATCC 35405 (black bars), T. denticola MHE (mid-grey bars), T. denticola CKE (dark-grey bars) and T. vincentii ATCC 35580

    Techniques Used:

    Fluorescence microscopy of monospecies or dual-species biofilms of T. denticola ATCC 35405, T. denticola CKE or T. denticola MHE, and P. gingivalis ATCC 33277, and corresponding biomass data. (a) Biofilms formed upon saliva-coated coverslips after 72
    Figure Legend Snippet: Fluorescence microscopy of monospecies or dual-species biofilms of T. denticola ATCC 35405, T. denticola CKE or T. denticola MHE, and P. gingivalis ATCC 33277, and corresponding biomass data. (a) Biofilms formed upon saliva-coated coverslips after 72

    Techniques Used: Fluorescence, Microscopy

    38) Product Images from "Treponema denticola chymotrypsin-like proteinase (CTLP) integrates spirochaetes within oral microbial communities"

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

    Journal: Microbiology

    doi: 10.1099/mic.0.055939-0

    Role of the CTLP complex in the formation of T. denticola / P. gingivalis dual-species biofilms. Representative CLSM images of dual-species biofilms of (a, b) T. denticola ATCC 35405 and (c, d) T. denticola CKE, with P. gingivalis ATCC 33277. Biofilms were
    Figure Legend Snippet: Role of the CTLP complex in the formation of T. denticola / P. gingivalis dual-species biofilms. Representative CLSM images of dual-species biofilms of (a, b) T. denticola ATCC 35405 and (c, d) T. denticola CKE, with P. gingivalis ATCC 33277. Biofilms were

    Techniques Used: Confocal Laser Scanning Microscopy

    Adherence levels of Treponema to other periodontopathogens. The input cell number was 1.2×10 7 cells per well of T. denticola ATCC 35405 (black bars), T. denticola MHE (mid-grey bars), T. denticola CKE (dark-grey bars) and T. vincentii ATCC 35580
    Figure Legend Snippet: Adherence levels of Treponema to other periodontopathogens. The input cell number was 1.2×10 7 cells per well of T. denticola ATCC 35405 (black bars), T. denticola MHE (mid-grey bars), T. denticola CKE (dark-grey bars) and T. vincentii ATCC 35580

    Techniques Used:

    Fluorescence microscopy of monospecies or dual-species biofilms of T. denticola ATCC 35405, T. denticola CKE or T. denticola MHE, and P. gingivalis ATCC 33277, and corresponding biomass data. (a) Biofilms formed upon saliva-coated coverslips after 72
    Figure Legend Snippet: Fluorescence microscopy of monospecies or dual-species biofilms of T. denticola ATCC 35405, T. denticola CKE or T. denticola MHE, and P. gingivalis ATCC 33277, and corresponding biomass data. (a) Biofilms formed upon saliva-coated coverslips after 72

    Techniques Used: Fluorescence, Microscopy

    39) Product Images from "Filamentous Actin Disruption and Diminished Inositol Phosphate Response in Gingival Fibroblasts Caused by Treponema denticola"

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

    Journal: Infection and Immunity

    doi:

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

    Techniques Used: Fluorescence, Labeling, Confocal Microscopy

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

    Techniques Used: Standard Deviation

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

    Techniques Used: SDS Page, Nucleic Acid Electrophoresis

    40) Product Images from "Filamentous Actin Disruption and Diminished Inositol Phosphate Response in Gingival Fibroblasts Caused by Treponema denticola"

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

    Journal: Infection and Immunity

    doi:

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

    Techniques Used: Fluorescence, Labeling, Confocal Microscopy

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

    Techniques Used: Standard Deviation

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

    Techniques Used: SDS Page, Nucleic Acid Electrophoresis

    Related Articles

    other:

    Article Title:
    Article Snippet: However, in our studies of T. denticola ATCC 35405, the Msp knockout mutant was unaffected in binding F. nucleatum .

    Article Title:
    Article Snippet: Cultures of T. denticola ATCC 35405 and mutant K1 were adjusted to an absorbance of 0.2 at 660 nm in TYGVS medium, and 1.0 ml of each was inoculated into 100 ml of TYGVS medium and incubated at 37°C under anaerobic conditions.

    Article Title:
    Article Snippet: The Treponema strains used in this study were T. denticola ATCC 35405 and GM-1 (from R. J. Lamont, University of Florida, Gainesville); T. vincentii ATCC 35580 and D2A-2 (from P. E. Greenberg, University of Iowa); and Treponema sp. strain UB1090 isolated from a sheep with contagious ovine digital dermatitis ( , ).

    Article Title:
    Article Snippet: Based on these findings, the 17 samples were divided into 2 distinct groups, A (15 samples) and B (the remaining 2), whose msp nucleotide sequences were closely related to T. denticola ATCC 35405 and ATCC 33520, respectively.

    Article Title:
    Article Snippet: T. denticola ATCC 35405 was propagated in TYGVS medium , while Porphyromonas gingivalis and Fusobacterium nucleatum were maintained on Tripticase soy agar (Becton Dickinson and Company, Cockeysville, Md.) containing 10% defribrinated horse blood, 5 μg of hemin per ml, and 0.5 μg of menadione per ml.

    Article Title:
    Article Snippet: T. denticola ATCC 35405 was inoculated into 500 ml of TYGVS medium and incubated for 3 days as described above.

    Article Title:
    Article Snippet: Neither proteinase inhibitor had an effect on the reduction in the yield of radiolabeled IPs when HGF were incubated with 1.0% FBS and whole cells of T. denticola ATCC 35405 (Table ).

    Article Title:
    Article Snippet: Receptor blocking experiments using rMsp from T. denticola ATCC 35405 confirmed that the N-terminal region of fibronectin is the only region targeted in vitro by T. denticola ATCC 35405.

    Article Title:
    Article Snippet: The msp gene of T. denticola ATCC 35405 may be divided into three coding regions on the basis of sequence conservation with msp of T. denticola ATCC 33520 (Fig. ).

    Article Title:
    Article Snippet: The recombinant plasmid was then linearized with Eco RI and Bgl II and electroporated into T. denticola ATCC 35405.

    Article Title:
    Article Snippet: The proteolytic activities of whole cells and sonic extracts from T. denticola ATCC 35405 and K1 were assayed with the synthetic chymotrypsin substrate SAAPNA.

    Article Title:
    Article Snippet: By using affinity chromatography, we detected a 100-kDa fibrinogen-binding protein in outer membrane extracts of T. denticola ATCC 35405.

    Article Title:
    Article Snippet: The detergent phase of Triton X-114 extracts from 1-liter batch cultures of T. denticola ATCC 35405 was subjected to preparative SDS-PAGE using a Model 491 Prep Cell (Bio-Rad Laboratories, Richmond, Calif.) as described previously ( ).

    Article Title:
    Article Snippet: The significantly diminished IP response to T. denticola ATCC 35405 occurred within 60 min, concomitant with significant reduction of total F-actin and disruption of stress fibers.

    Article Title:
    Article Snippet: Native Msp was purified by preparative electrophoresis from 4-liter batch cultures of T. denticola ATCC 35405 as described previously , with minor modifications.

    Article Title:
    Article Snippet: To determine the effects of these region-specific antibodies on bacterial adhesion, biotinylated cells of T. denticola ATCC 35405 were preincubated with a range of dilutions of antiserum or preimmune serum (control).

    Article Title:
    Article Snippet: Notably, sequence analysis of the entire msp gene in all 17 samples showed that the 5'region, encompassing base pairs 1-600, was 99% homologous to that of T. denticola ATCC 35405 and ATCC 33520, as was observed for the 3' region, comprising nucleotides 900-1632.

    Article Title:
    Article Snippet: A prominent 70-kDa protein was isolated from surface extracts of T. denticola ATCC 35405.

    Article Title:
    Article Snippet: The Msp proteins from T. denticola ATCC 35405 and ATCC 35520 show high sequence identity (except for the central V region; Fig. ), whereas the Msp polypeptide from T. denticola OTK is significantly different and antigenically distinct ( ).

    Article Title:
    Article Snippet: T. vincentii showed a different coaggregation profile from that of T. denticola ATCC 35405.

    Article Title:
    Article Snippet: An erythromycin resistance cassette was then inserted at the confluence of these two fragments, in place of the proteolytic domain, generating pISHI102. pISHI102 was then linearized with Eco RI, and used to transform T. denticola ATCC 35405 by electroporation.

    Article Title:
    Article Snippet: To achieve this we conducted ideT -specific RT-PCR using mRNA from a late-exponential phase culture of T. denticola ATCC 35405, and primer pair IDEAF and IDEAR, which anneal at 171–197 bp and 1766–1792 bp of the ideT open reading frame.

    Article Title:
    Article Snippet: The SAAPFNA activity expressed by strain CKE cells was not above background levels, suggesting that CTLP accounts for the total chymotrypsin-like activity of T. denticola ATCC 35405.

    Article Title:
    Article Snippet: The inclusion of PMSF resulted in the enhanced binding of T. denticola ATCC 35405 to both fluid-phase (Fig. ) and immobilized (Fig. ) fibrinogen.

    Article Title:
    Article Snippet: Thus, T. denticola ATCC 35405 was able to bind fibrinogen in either the fluid or the solid phase, and the relative binding levels were not markedly different within the limitations of the assays.

    Article Title:
    Article Snippet: An amplified fragment of 699 bp , using primer pair ID-1/CATU was generated from late-exponential phase mRNA of T. denticola ATCC 35405, indicating that the ideT transcript, encompassing the dentipain domain, is expressed during growth of this organism.

    Article Title:
    Article Snippet: Briefly, T. denticola ATCC 35405 and K1 were grown for 72 h under anaerobic conditions as described above and harvested.

    Article Title:
    Article Snippet: Genomic DNAs from T. denticola ATCC 35405 and K1 were isolated and hybridization was performed as described previously ( ).

    Article Title:
    Article Snippet: As shown in , antibodies raised against a recombinant N-terminal fragment of Msp (residues 14 to 202) recognized all of the recombinant Msp deletion constructs expressed in E. coli , as well as native Msp from T. denticola ATCC 35405.

    Article Title:
    Article Snippet: This might be explained by suggesting that vacant sites were available on the surface of these strains to acquire exogenously supplied Msp molecules, whereas these could not be incorporated at elevated levels onto the surface of T. denticola ATCC 35405 or GM-1.

    Article Title:
    Article Snippet: Inhibition by rMsp was dose dependent up to a maximum of 40% for binding to fibronectin and to 60% inhibition of cell binding to the 30-kDa fragment (Fig. ). rMsp from T. denticola ATCC 35405 was also effective in inhibiting adhesion of T. denticola GM-1 cells to immobilized fibronectin and the 30-kDa fragment (Fig. ).

    Article Title:
    Article Snippet: However, levels of adherence of T. denticola ATCC 35405 and MHE cells to fibrinogen were significantly enhanced following the pretreatment of cells with PMSF.

    Article Title:
    Article Snippet: Kolenbrander et al. ( ) reported visible coaggregation between F. nucleatum and T. denticola ATCC 35405.

    Article Title:
    Article Snippet: In this study we have identified a protein ortholog of IdeS in the genome of T. denticola ATCC 35405, and demonstrated that it is indeed a functional protease which significantly contributes to the pathogenesis of T. denticola .

    Article Title:
    Article Snippet: This PMSF concentration was sufficient to inhibit > 95% of the chymotrypsin-like activity of T. denticola ATCC 35405, as determined by a SAAPFNA assay.

    Article Title:
    Article Snippet: Although previous work has demonstrated the adherence of T. denticola to immobilized fibrinogen , the present study provides evidence that T. denticola ATCC 35405 binds both fluid-phase and immobilized fibrinogen and provides a molecular basis for these interactions.

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  • 93
    ATCC t denticola atcc 35405
    TCT in the absence or presence of T. <t>denticola</t> ATCC 35405, MHE (Msp − ), or CKE (CTLP − ). Human plasma was incubated with T. denticola (1.2 × 10 9 cells/ml) suspended in PBS or with PBS alone (control) for 5 min before the addition
    T Denticola Atcc 35405, supplied by ATCC, used in various techniques. Bioz Stars score: 93/100, based on 11 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/t denticola atcc 35405/product/ATCC
    Average 93 stars, based on 11 article reviews
    Price from $9.99 to $1999.99
    t denticola atcc 35405 - by Bioz Stars, 2020-01
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    90
    ATCC t denticola atcc 35405 cells
    TCT in the absence or presence of T. <t>denticola</t> ATCC 35405, MHE (Msp − ), or CKE (CTLP − ). Human plasma was incubated with T. denticola (1.2 × 10 9 cells/ml) suspended in PBS or with PBS alone (control) for 5 min before the addition
    T Denticola Atcc 35405 Cells, supplied by ATCC, used in various techniques. Bioz Stars score: 90/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/t denticola atcc 35405 cells/product/ATCC
    Average 90 stars, based on 2 article reviews
    Price from $9.99 to $1999.99
    t denticola atcc 35405 cells - by Bioz Stars, 2020-01
    90/100 stars
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    TCT in the absence or presence of T. denticola ATCC 35405, MHE (Msp − ), or CKE (CTLP − ). Human plasma was incubated with T. denticola (1.2 × 10 9 cells/ml) suspended in PBS or with PBS alone (control) for 5 min before the addition

    Journal: Infection and Immunity

    Article Title: The Chymotrypsin-Like Protease Complex of Treponema denticola ATCC 35405 Mediates Fibrinogen Adherence and Degradation ▿

    doi: 10.1128/IAI.00258-07

    Figure Lengend Snippet: TCT in the absence or presence of T. denticola ATCC 35405, MHE (Msp − ), or CKE (CTLP − ). Human plasma was incubated with T. denticola (1.2 × 10 9 cells/ml) suspended in PBS or with PBS alone (control) for 5 min before the addition

    Article Snippet: Although previous work has demonstrated the adherence of T. denticola to immobilized fibrinogen , the present study provides evidence that T. denticola ATCC 35405 binds both fluid-phase and immobilized fibrinogen and provides a molecular basis for these interactions.

    Techniques: Incubation

    Fibrinogen zymograms of outer membrane proteins from T. denticola ATCC 35405, MHE (Msp − ), and CKE (CTLP − ). Triton X-114 extracts were incubated for 5 min at 20°C (−) or 100°C (+) before being subjected to

    Journal: Infection and Immunity

    Article Title: The Chymotrypsin-Like Protease Complex of Treponema denticola ATCC 35405 Mediates Fibrinogen Adherence and Degradation ▿

    doi: 10.1128/IAI.00258-07

    Figure Lengend Snippet: Fibrinogen zymograms of outer membrane proteins from T. denticola ATCC 35405, MHE (Msp − ), and CKE (CTLP − ). Triton X-114 extracts were incubated for 5 min at 20°C (−) or 100°C (+) before being subjected to

    Article Snippet: Although previous work has demonstrated the adherence of T. denticola to immobilized fibrinogen , the present study provides evidence that T. denticola ATCC 35405 binds both fluid-phase and immobilized fibrinogen and provides a molecular basis for these interactions.

    Techniques: Incubation

    Purification and enzymatic activity of major fibrinogen-binding protein from T. denticola ATCC 35405. Outer membrane proteins were extracted with 0.1% Triton X-114 solution and incubated with fibrinogen-linked Sepharose, and then tightly bound

    Journal: Infection and Immunity

    Article Title: The Chymotrypsin-Like Protease Complex of Treponema denticola ATCC 35405 Mediates Fibrinogen Adherence and Degradation ▿

    doi: 10.1128/IAI.00258-07

    Figure Lengend Snippet: Purification and enzymatic activity of major fibrinogen-binding protein from T. denticola ATCC 35405. Outer membrane proteins were extracted with 0.1% Triton X-114 solution and incubated with fibrinogen-linked Sepharose, and then tightly bound

    Article Snippet: Although previous work has demonstrated the adherence of T. denticola to immobilized fibrinogen , the present study provides evidence that T. denticola ATCC 35405 binds both fluid-phase and immobilized fibrinogen and provides a molecular basis for these interactions.

    Techniques: Purification, Activity Assay, Binding Assay, Incubation

    Binding of fluid-phase or immobilized fibrinogen by T. denticola ATCC 35405 (⧫), MHE (Msp − ; ▴), or CKE (CTLP − ; ▪). (A and B) Treponema cells immobilized onto plastic wells in the absence (A) or presence (B) of 0.05

    Journal: Infection and Immunity

    Article Title: The Chymotrypsin-Like Protease Complex of Treponema denticola ATCC 35405 Mediates Fibrinogen Adherence and Degradation ▿

    doi: 10.1128/IAI.00258-07

    Figure Lengend Snippet: Binding of fluid-phase or immobilized fibrinogen by T. denticola ATCC 35405 (⧫), MHE (Msp − ; ▴), or CKE (CTLP − ; ▪). (A and B) Treponema cells immobilized onto plastic wells in the absence (A) or presence (B) of 0.05

    Article Snippet: Although previous work has demonstrated the adherence of T. denticola to immobilized fibrinogen , the present study provides evidence that T. denticola ATCC 35405 binds both fluid-phase and immobilized fibrinogen and provides a molecular basis for these interactions.

    Techniques: Binding Assay

    Fibrinogen blot overlay of outer membrane protein extracts from T. denticola ATCC 35405, MHE, and CKE. Proteins were extracted with 1% Triton X-114 and incubated for 5 min at 20°C (−) or 100°C (+) before being subjected

    Journal: Infection and Immunity

    Article Title: The Chymotrypsin-Like Protease Complex of Treponema denticola ATCC 35405 Mediates Fibrinogen Adherence and Degradation ▿

    doi: 10.1128/IAI.00258-07

    Figure Lengend Snippet: Fibrinogen blot overlay of outer membrane protein extracts from T. denticola ATCC 35405, MHE, and CKE. Proteins were extracted with 1% Triton X-114 and incubated for 5 min at 20°C (−) or 100°C (+) before being subjected

    Article Snippet: Although previous work has demonstrated the adherence of T. denticola to immobilized fibrinogen , the present study provides evidence that T. denticola ATCC 35405 binds both fluid-phase and immobilized fibrinogen and provides a molecular basis for these interactions.

    Techniques: Incubation

    Adherence of T. denticola ATCC 35405 cells to denatured fibrinogen or recombinant fibrinogen polypeptides. (A) Human fibrinogen (N) or purified recombinant Aα, Bβ, and γ chain polypeptides were heated for 5 min at 100°C

    Journal: Infection and Immunity

    Article Title: The Chymotrypsin-Like Protease Complex of Treponema denticola ATCC 35405 Mediates Fibrinogen Adherence and Degradation ▿

    doi: 10.1128/IAI.00258-07

    Figure Lengend Snippet: Adherence of T. denticola ATCC 35405 cells to denatured fibrinogen or recombinant fibrinogen polypeptides. (A) Human fibrinogen (N) or purified recombinant Aα, Bβ, and γ chain polypeptides were heated for 5 min at 100°C

    Article Snippet: Although previous work has demonstrated the adherence of T. denticola to immobilized fibrinogen , the present study provides evidence that T. denticola ATCC 35405 binds both fluid-phase and immobilized fibrinogen and provides a molecular basis for these interactions.

    Techniques: Recombinant, Purification

    TCT in the absence or presence of T. denticola ATCC 35405, MHE (Msp − ), or CKE (CTLP − ). Human plasma was incubated with T. denticola (1.2 × 10 9 cells/ml) suspended in PBS or with PBS alone (control) for 5 min before the addition

    Journal: Infection and Immunity

    Article Title: The Chymotrypsin-Like Protease Complex of Treponema denticola ATCC 35405 Mediates Fibrinogen Adherence and Degradation ▿

    doi: 10.1128/IAI.00258-07

    Figure Lengend Snippet: TCT in the absence or presence of T. denticola ATCC 35405, MHE (Msp − ), or CKE (CTLP − ). Human plasma was incubated with T. denticola (1.2 × 10 9 cells/ml) suspended in PBS or with PBS alone (control) for 5 min before the addition

    Article Snippet: The binding of fluid-phase fibrinogen by T. denticola ATCC 35405 cells was dose dependent and saturable up to a maximum of 1 μg of added fibrinogen (Fig. ).

    Techniques: Incubation

    Fibrinogen zymograms of outer membrane proteins from T. denticola ATCC 35405, MHE (Msp − ), and CKE (CTLP − ). Triton X-114 extracts were incubated for 5 min at 20°C (−) or 100°C (+) before being subjected to

    Journal: Infection and Immunity

    Article Title: The Chymotrypsin-Like Protease Complex of Treponema denticola ATCC 35405 Mediates Fibrinogen Adherence and Degradation ▿

    doi: 10.1128/IAI.00258-07

    Figure Lengend Snippet: Fibrinogen zymograms of outer membrane proteins from T. denticola ATCC 35405, MHE (Msp − ), and CKE (CTLP − ). Triton X-114 extracts were incubated for 5 min at 20°C (−) or 100°C (+) before being subjected to

    Article Snippet: The binding of fluid-phase fibrinogen by T. denticola ATCC 35405 cells was dose dependent and saturable up to a maximum of 1 μg of added fibrinogen (Fig. ).

    Techniques: Incubation

    Purification and enzymatic activity of major fibrinogen-binding protein from T. denticola ATCC 35405. Outer membrane proteins were extracted with 0.1% Triton X-114 solution and incubated with fibrinogen-linked Sepharose, and then tightly bound

    Journal: Infection and Immunity

    Article Title: The Chymotrypsin-Like Protease Complex of Treponema denticola ATCC 35405 Mediates Fibrinogen Adherence and Degradation ▿

    doi: 10.1128/IAI.00258-07

    Figure Lengend Snippet: Purification and enzymatic activity of major fibrinogen-binding protein from T. denticola ATCC 35405. Outer membrane proteins were extracted with 0.1% Triton X-114 solution and incubated with fibrinogen-linked Sepharose, and then tightly bound

    Article Snippet: The binding of fluid-phase fibrinogen by T. denticola ATCC 35405 cells was dose dependent and saturable up to a maximum of 1 μg of added fibrinogen (Fig. ).

    Techniques: Purification, Activity Assay, Binding Assay, Incubation

    Binding of fluid-phase or immobilized fibrinogen by T. denticola ATCC 35405 (⧫), MHE (Msp − ; ▴), or CKE (CTLP − ; ▪). (A and B) Treponema cells immobilized onto plastic wells in the absence (A) or presence (B) of 0.05

    Journal: Infection and Immunity

    Article Title: The Chymotrypsin-Like Protease Complex of Treponema denticola ATCC 35405 Mediates Fibrinogen Adherence and Degradation ▿

    doi: 10.1128/IAI.00258-07

    Figure Lengend Snippet: Binding of fluid-phase or immobilized fibrinogen by T. denticola ATCC 35405 (⧫), MHE (Msp − ; ▴), or CKE (CTLP − ; ▪). (A and B) Treponema cells immobilized onto plastic wells in the absence (A) or presence (B) of 0.05

    Article Snippet: The binding of fluid-phase fibrinogen by T. denticola ATCC 35405 cells was dose dependent and saturable up to a maximum of 1 μg of added fibrinogen (Fig. ).

    Techniques: Binding Assay

    Fibrinogen blot overlay of outer membrane protein extracts from T. denticola ATCC 35405, MHE, and CKE. Proteins were extracted with 1% Triton X-114 and incubated for 5 min at 20°C (−) or 100°C (+) before being subjected

    Journal: Infection and Immunity

    Article Title: The Chymotrypsin-Like Protease Complex of Treponema denticola ATCC 35405 Mediates Fibrinogen Adherence and Degradation ▿

    doi: 10.1128/IAI.00258-07

    Figure Lengend Snippet: Fibrinogen blot overlay of outer membrane protein extracts from T. denticola ATCC 35405, MHE, and CKE. Proteins were extracted with 1% Triton X-114 and incubated for 5 min at 20°C (−) or 100°C (+) before being subjected

    Article Snippet: The binding of fluid-phase fibrinogen by T. denticola ATCC 35405 cells was dose dependent and saturable up to a maximum of 1 μg of added fibrinogen (Fig. ).

    Techniques: Incubation

    Adherence of T. denticola ATCC 35405 cells to denatured fibrinogen or recombinant fibrinogen polypeptides. (A) Human fibrinogen (N) or purified recombinant Aα, Bβ, and γ chain polypeptides were heated for 5 min at 100°C

    Journal: Infection and Immunity

    Article Title: The Chymotrypsin-Like Protease Complex of Treponema denticola ATCC 35405 Mediates Fibrinogen Adherence and Degradation ▿

    doi: 10.1128/IAI.00258-07

    Figure Lengend Snippet: Adherence of T. denticola ATCC 35405 cells to denatured fibrinogen or recombinant fibrinogen polypeptides. (A) Human fibrinogen (N) or purified recombinant Aα, Bβ, and γ chain polypeptides were heated for 5 min at 100°C

    Article Snippet: The binding of fluid-phase fibrinogen by T. denticola ATCC 35405 cells was dose dependent and saturable up to a maximum of 1 μg of added fibrinogen (Fig. ).

    Techniques: Recombinant, Purification