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首页> 外文期刊>Infection and immunity >Binding Properties and Adhesion-Mediating Regions of the Major Sheath Protein of Treponema denticola ATCC 35405
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Binding Properties and Adhesion-Mediating Regions of the Major Sheath Protein of Treponema denticola ATCC 35405

机译：Treponema Denticola ATCC 35405主要护套蛋白的结合特性和粘附介化区域

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There is growing evidence that a number of oral Treponema species, in particular Treponema denticola, are associated with the progression of human periodontal disease. The major sheath (or surface) protein (Msp) of T. denticola is implicated in adhesion of bacteria to host cells and tissue proteins and is likely to be an important virulence factor. However, the binding regions of the Msp are not known. We have purified from Escherichia coli recombinant Msp (rMsp) polypeptides corresponding to the following: full-length Msp (rMsp) minus 13 N-terminal amino acid (aa) residues, an amino-terminal fragment (rN-Msp, 189 aa residues), a 57-aa residue segment from the central region (rV-Msp), and a C-terminal fragment (rC-Msp, 272 aa residues). rMsp (530 aa residues) bound to immobilized fibronectin, keratin, laminin, collagen type I, fibrinogen, hyaluronic acid, and heparin. The N- and V-region polypeptides, but not rC-Msp, also bound to these substrates. Binding of rMsp to fibronectin was targeted to the N-terminal heparin I/fibrin I domain. Antibodies to the N-region or V-region polypeptides, but not antibodies to the rC-Msp fragment, blocked adhesion of T. denticola ATCC 35405 cells to a range of host protein molecules. These results suggest that the N-terminal half of Msp carries epitopes that are surface exposed and that are involved in mediating adhesion. Binding of rMsp onto the cell surface of low-level fibronectin-binding Treponema isolates conferred a 10-fold increase in fibronectin binding. This confirms that Msp functions autonomously as an adhesin and raises the possibility that phenotypic complementation of virulence functions might occur within mixed populations of Treponema species.
机译：还有日益增长的证据表明，许多口腔串口物种，特别是 treponemadenticola ，与人类牙周病的进展相关。 T的主要护套（或表面）蛋白（MSP）。牙霉素涉及细菌对宿主细胞和组织蛋白质的粘附性，并且可能是一个重要的毒力因子。然而，MSP的结合区域是未知的。我们已经纯化了对应于以下内容的大肠杆菌（RMSP）多肽（RMSP）多肽：全长MSP（RMSP）减去13 N-末端氨基酸（AA）残基，氨基末端片段（RN -MSP，189AA残基），来自中心区域（RV-MSP）的57-AA残基分段，以及C末端片段（RC-MSP，272 AA残基）。 RMSP（530 AA残基）与固定的纤连蛋白，角蛋白，层蛋白，胶原蛋白I，纤维蛋白原，透明质酸和肝素结合。 N-和V区多肽，但不是RC-MSP，也与这些基材结合。 RMSP与纤连蛋白的结合靶向N-末端肝素I /纤维蛋白I结构域。对N区或V区多肽的抗体，但不具有对RC-MSP片段的抗体，抑制 T的粘附性。牙本菌 ATCC 35405细胞到一系列宿主蛋白质分子。这些结果表明，MSP的N-末端半部携带表面暴露的表位，并且参与介导的粘合性。 RMSP与低水平纤连蛋白结合物的细胞表面的结合赋予纤维蛋白结合的10倍增加10倍。这证实了MSP作为粘附素自主函数，并提高了毒力功能的表型互补的可能性可能发生在 Treponema 物种的混合群体中。

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