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首页> 外文期刊>Infection and immunity >Tyrosine Phosphorylation of the Chlamydial Effector Protein Tarp Is Species Specific and Not Required for Recruitment of Actin
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Tyrosine Phosphorylation of the Chlamydial Effector Protein Tarp Is Species Specific and Not Required for Recruitment of Actin

机译：衣原体效应蛋白篷布的酪氨酸磷酸化是特定物种，不需要肌动蛋白的招聘。

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Chlamydiae are obligate intracellular pathogens that efficiently induce their endocytosis by susceptible eukaryotic host cells. Recently, a Chlamydia trachomatis type III secreted effector protein, Tarp, was found to be translocated and tyrosine phosphorylated at the site of entry and associated with the recruitment of actin that coincides with endocytosis. C. trachomatis Tarp possesses up to six direct repeats of approximately 50 amino acids each. The majority of the tyrosine residues are found within this repeat region. Here we have ectopically expressed distinct domains of Tarp in HeLa 229 cells and demonstrated that tyrosine phosphorylation occurs primarily within the repeat region, while recruitment of actin is mediated by the C-terminal domain of the protein. A comparison of other sequenced chlamydial genomes revealed that each contains an ortholog of Tarp, although Chlamydia muridarum, Chlamydophila caviae, and Chlamydophila pneumoniae Tarp lack the large repeat region. Immunofluorescence and immunoblotting using an antiphosphotyrosine antibody show no evidence of phosphotyrosine at the site of entry of C. muridarum, C. caviae, and C. pneumoniae, although each species similarly recruits actin. Ectopic expression of full-length C. trachomatis and C. caviae Tarp confirmed that both recruit actin but only C. trachomatis Tarp is tyrosine phosphorylated. The data indicate that the C-terminal domain of Tarp is essential for actin recruitment and that tyrosine phosphorylation may not be an absolute requirement for actin recruitment. The results further suggest the potential for additional, unknown signal transduction pathways associated specifically with C. trachomatis.
机译：衣原体是专性的细胞内病原体，其通过易感的真核宿主细胞有效诱导其胞吞作用。最近，发现一种沙眼衣原体分泌型效应蛋白Tarp在进入位点易位并酪氨酸磷酸化，并与肌动蛋白的募集有关，这与胞吞作用一致。 C。沙眼Tarp最多具有六个直接重复，每个重复约50个氨基酸。在该重复区域内发现大多数酪氨酸残基。在这里，我们在HeLa 229细胞中异位表达了Tarp的不同结构域，并证明酪氨酸磷酸化主要发生在重复区域内，而肌动蛋白的募集则由该蛋白的C末端结构域介导。对其他测序的衣原体基因组进行比较后发现，虽然 muridarum ，衣原体衣原体和肺炎衣原体都没有Tarp直系同源基因。大的重复区域。使用抗磷酸酪氨酸抗体的免疫荧光和免疫印迹显示在C进入位点没有磷酸酪氨酸的证据。 muridarum ， C。 caviae 和 C。肺炎，尽管每个物种都相似地募集肌动蛋白。全长 C的异位表达。沙眼和 C。 caviae Tarp证实，它们都募集肌动蛋白，但仅募集C。沙眼tarp被酪氨酸磷酸化。数据表明，Tarp的C末端结构域对于肌动蛋白募集至关重要，酪氨酸磷酸化可能不是肌动蛋白募集的绝对要求。结果进一步表明了可能存在与 C特异性相关的其他未知信号转导途径。沙眼。

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