Actin and intermediate filaments stabilize the Chlamydia trachomatis vacuole by forming dynamic structural scaffolds.
Actin and intermediate filaments stabilize the Chlamydia trachomatis vacuole by forming dynamic structural scaffolds.
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DOI：
10.1016/j.chom.2008.05.018
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发表时间：
2008-08-14
影响因子：
30.3
通讯作者：
Valdivia RH
中科院分区：
文献类型：
--
作者：
Kumar Y;Valdivia RH
沙眼衣原体在一个大液泡中复制(“包涵体”)，它将细菌成分隔离在与宿主细胞质的直接接触中。在这里，我们报告包涵体被包裹在F-肌动蛋白和中间丝(IF)的网络中，这些支架结构为后生动物细胞提供机械支持，这些细胞骨架结构协同作用稳定含有病原体的空泡。F-肌动蛋白在包涵体上的形成依赖于RhoA，它的破坏导致IFs的解体、包涵体完整性的丧失和包涵体内容物泄漏到宿主细胞质中。此外，如果蛋白质被分泌的衣原体蛋白水解酶CPAF处理，在包涵体表面形成丝状结构，结构性质发生变化。我们认为衣原体结合了F-肌动蛋白和迭代函数系统的功能，通过一个动态的结构支架来稳定包涵体，同时最大限度地减少包涵体内容对细胞质天然免疫监视途径的暴露。
Chlamydia trachomatis replicates within a large vacuole (“inclusion”) that sequesters bacterial components from direct contact with the host cytoplasm. Here, we report that the inclusion is encased in a network of F-actin and intermediate filaments (IF), scaffolding structures that provide mechanical support to metazoan cells, and that these cytoskeletal structures act cooperatively to stabilize the pathogen-containing vacuole. Formation of F-actin at the inclusion was dependent on RhoA and its disruption led to the disassembly of IFs, loss of inclusion integrity and leakage of inclusion contents into the host cytoplasm. In addition, IF proteins were processed by the secreted chlamydial protease CPAF to form filamentous structures at the inclusion surface with altered structural properties. We propose that Chlamydia has co-opted the function of F-actin and IFs to stabilize the inclusion with a dynamic, structural scaffold while minimizing the exposure of inclusion contents to cytoplasmic innate immune surveillance pathways.
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