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首页> 外文期刊>Infection and immunity >Topology of Legionella pneumophila DotA: an inner membrane protein required for replication in macrophages.
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Topology of Legionella pneumophila DotA: an inner membrane protein required for replication in macrophages.

机译：肺炎军团菌DotA拓扑：在巨噬细胞中复制所需的内膜蛋白。

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The Legionella pneumophila dotA gene is required for intracellular growth of the bacterium in macrophages. In this study, a structure-function analysis of the DotA protein was conducted to elucidate the role of this protein in L. pneumophila pathogenesis. Translational fusions of dotA to the Escherichia coli phoA and lacZ genes indicated that DotA is an integral cytoplasmic membrane protein with eight membrane-spanning domains. DotA contains two large periplasmic domains of approximately 503 and 73 amino acids and a carboxyl-terminal cytoplasmic domain of 122 amino acids. Protein fractionation studies were consistent with DotA residing in the inner membrane. An alkaline phosphatase fusion located 9 amino acids upstream from the C terminus of DotA still retained function and was able to restore intracellular growth when harbored by two L. pneumophila dotA mutants. A hybrid protein from which the carboxyl-terminal 48 amino acids of DotA were deleted was unable to complement the intracellular growth defect in the dotA mutants, indicating that this cytoplasmic region is required for function.
机译：嗜肺军团菌dotA基因是细菌在巨噬细胞中细胞内生长所必需的。在这项研究中，进行了DotA蛋白的结构功能分析，以阐明该蛋白在嗜肺乳杆菌的发病机理中的作用。 dotA与大肠杆菌phoA和lacZ基因的翻译融合表明DotA是具有八个跨膜结构域的完整胞质膜蛋白。 DotA包含两个大约503和73个氨基酸的大周质结构域和一个122个氨基酸的羧基末端细胞质结构域。蛋白质分离研究与内膜中的DotA一致。位于DotA C末端上游9个氨基酸处的碱性磷酸酶融合体仍保留功能，并且在被两个嗜肺乳杆菌dotA突变体掩藏时能够恢复细胞内生长。 DotA的羧基末端48个氨基酸被删除的杂合蛋白无法弥补dotA突变体中的细胞内生长缺陷，表明该细胞质区域是功能所必需的。

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