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首页> 外文期刊>Infection and immunity >Novel Surface Structures Are Associated with the Adhesion of Actinobacillus actinomycetemcomitans to Collagen
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Novel Surface Structures Are Associated with the Adhesion of Actinobacillus actinomycetemcomitans to Collagen

机译：新型表面结构与放线放线杆菌对胶原蛋白的粘附有关。

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Actinobacillus actinomycetemcomitans is a gram-negative, facultative, anaerobic bacterium that colonizes the human oral cavity and the upper respiratory tract. This bacterium is strongly associated with localized aggressive periodontitis and adult periodontitis and is the causative agent for other serious systemic infections. Recently, we have identified a protein, EmaA (extracellular matrix protein adhesin A), that mediates the adhesion of A. actinomycetemcomitans to collagen. The conserved sequence and predicted secondary structure suggest that EmaA is an orthologue of the Yersinia enterocolitica adhesin YadA. Electron microscopy examinations of A. actinomycetemcomitans have identified antenna-like protrusions associated with the surface of the bacterium. These structures are absent on emaA mutant strains and can be restored by transformation of the mutant strain with emaA in trans. The loss of these structures is associated with a decrease in the binding of this bacterium to collagen. The antenna-like structures are composed of a long rod that terminates in an ellipsoidal head region. The analysis of these structures using image processing techniques has provided an initial estimate of the overall dimensions, which suggests that the appendages are oligomeric structures formed by either three or four subunits. Together, the data suggest that emaA is required for the expression of novel appendages on the surface of A. actinomycetemcomitans that mediate the adhesion of the bacterium to collagen.
机译：放线杆菌放线杆菌是一种革兰氏阴性，兼性厌氧细菌，定居于人类口腔和上呼吸道。该细菌与局部侵袭性牙周炎和成人牙周炎密切相关，是其他严重全身感染的病原体。最近，我们已经鉴定出一种蛋白EmaA（细胞外基质蛋白粘附素A），它介导 A的粘附。放线菌对胶原蛋白的作用。保守的序列和预期的二级结构表明，EmaA是 Enterocolitica 黏附素YadA的直向同源物。 A的电子显微镜检查。放线菌已经鉴定出与细菌表面相关的触角状突起。这些结构在 emaA 突变菌株中不存在，可以通过在 trans 中用 emaA 转化突变菌株来恢复。这些结构的丧失与该细菌与胶原蛋白的结合减少有关。天线状结构由终止于椭圆形头部区域的长杆组成。使用图像处理技术对这些结构的分析提供了整体尺寸的初步估计，这表明这些附属物是由三个或四个亚基形成的寡聚结构。总之，数据表明 emaA 是在 A表面表达新型附件所必需的。放线菌，介导细菌与胶原的粘附。

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