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首页> 外文期刊>Infection and immunity >The integrin-binding domain of invasin is sufficient to allow bacterial entry into mammalian cells.
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The integrin-binding domain of invasin is sufficient to allow bacterial entry into mammalian cells.

机译：侵入蛋白的整联蛋白结合结构域足以允许细菌进入哺乳动物细胞。

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摘要

Yersinia pseudotuberculosis is able to enter normally nonphagocytic host cells by multiple pathways, the most efficient of which is mediated by invasin, a 986-amino-acid bacterial outer membrane protein. It has previously been shown that the C-terminal 192 amino acids of invasin are sufficient to bind mammalian cells. To determine if additional regions of the invasin protein are necessary to promote entry, we developed a novel assay that tests the ability of various invasin derivatives to confer on Staphylococcus aureus the ability to enter animal cells. We determined that the 192-amino-acid cell-binding region of invasin, when used to coat the bacterial cell surface, was also sufficient to promote cellular penetration. These results suggest that the simple binding of invasin to its receptors is sufficient to mediate entry and that the bacterium plays a largely passive role in the entry process.
机译：伪结核耶尔森氏菌能够通过多种途径进入正常的非吞噬性宿主细胞，其中最有效的途径是由986个氨基酸的细菌外膜蛋白入侵素介导的。先前已经显示，入侵素的C-末端192个氨基酸足以结合哺乳动物细胞。为了确定是否需要其他invasin蛋白区域来促进进入，我们开发了一种新颖的检测方法，用于测试各种invasin衍生物赋予金黄色葡萄球菌进入动物细胞的能力。我们确定，当侵染素的192个氨基酸细胞结合区用于覆盖细菌细胞表面时，也足以促进细胞渗透。这些结果表明，入侵素与其受体的简单结合足以介导进入，并且该细菌在进入过程中起很大的被动作用。

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