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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >A chlamydial type Ⅲ translocated protein is tyrosine-phosphorylated at the site of entry and associated with recruitment of actin
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A chlamydial type Ⅲ translocated protein is tyrosine-phosphorylated at the site of entry and associated with recruitment of actin

机译：衣原体Ⅲ型移位蛋白在进入位点被酪氨酸磷酸化并与肌动蛋白的募集有关

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摘要

The obligate intracellular bacterium Chlamydia trachomatis rapidly induces its own entry into host cells. Initial attachment is mediated by electrostatic interactions to heparan sulfate moieties on the host cell, followed by irreversible binding to an unknown secondary receptor. This secondary binding leads to the recruitment of actin to the site of attachment, formation of an actin-rich, pedestal-like structure, and finally internalization of the bacteria. How chlamydiae induce this process is unknown. We have identified a high-molecular-mass tyrosine-phosphorylated protein that is rapidly phosphorylated on attachment to the host cell. Immunoelec-tron microscopy studies revealed that this tyrosine-phosphorylated protein is localized to the cytoplasmic face of the plasma membrane at the site of attachment of surface-associated chlamydiae. The phosphoprotein was isolated by immunoprecipitation with the antiphosphotyrosine antibody 4G10 and identified as the chlamydial protein CT456, a hypothetical protein with unknown function. The chlamydial protein (Tarp) appears to be translocated into the host cell by type Ⅲ secretion because it is exported in a Yersinia heterologous expression assay. Phosphotyrosine signaling across the plasma membrane preceded the recruitment of actin to the site of chlamydial attachment and may represent the initial signal transduced from pathogen to the host cell. These results suggest that C trachomatis internalization is mediated by a chlamydial type Ⅲ-secreted effector protein.
机译：专性细胞内细菌沙眼衣原体迅速诱导其自身进入宿主细胞。最初的附着是通过与宿主细胞上硫酸乙酰肝素部分的静电相互作用介导的，然后不可逆地结合至未知的次级受体。这种次级结合导致肌动蛋白募集到附着位点，形成富含肌动蛋白的，类似基座的结构，并最终使细菌内化。衣原体如何诱导该过程尚不清楚。我们已经鉴定出一种高分子量的酪氨酸磷酸化蛋白，该蛋白在附着于宿主细胞后迅速被磷酸化。免疫电子-tron显微镜研究表明，这种酪氨酸磷酸化的蛋白位于与表面相关的衣原体附着部位的质膜胞质面上。通过用抗磷酸酪氨酸抗体4G10进行免疫沉淀分离出磷蛋白，并将其鉴定为衣原体蛋白CT456，这是一种功能未知的假定蛋白。衣原体蛋白（Tarp）似乎通过Ⅲ型分泌转移到宿主细胞中，因为它在耶尔森氏菌异源表达试验中被输出。跨质膜的磷酸酪氨酸信号在肌动蛋白募集到衣原体附着位点之前发生，可能代表了从病原体转导到宿主细胞的初始信号。这些结果表明沙眼衣原体的内在化是由衣原体Ⅲ型分泌效应蛋白介导的。

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