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首页> 外文期刊>Infection and immunity >Establishment of Unipolar Localization of IcsA in Shigella flexneri 2a Is Not Dependent on Virulence Plasmid Determinants
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Establishment of Unipolar Localization of IcsA in Shigella flexneri 2a Is Not Dependent on Virulence Plasmid Determinants

机译：弗氏志贺氏菌2a中IcsA的单极定位的建立并不依赖于毒力质粒决定因素。

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Unipolar localization of IcsA on the surface of Shigella flexneri is required for efficient formation of actin tails and protrusions in infected eucaryotic cells. Lipopolysaccharide (LPS) mutations have been demonstrated to affect either the establishment or the maintenance of IcsA in a unipolar location, although the mechanism is unknown. In order to analyze the contribution of virulence plasmid determinants on the unipolar localization of IcsA, we examined the localization of IcsA expressed from a cloned plasmid copy in two different genetic backgrounds. The localization of IcsA was first examined in a virulence plasmid-cured derivative of the wild-typeS. flexneri 2a isolate 2457T. This approach examined the contribution of virulence plasmid-borne factors, including the previously identified virulence plasmid-borne protease that is responsible for cleaving IcsA in the outer membrane and releasing the 95-kDa secreted form from the cell surface. IcsA localization in a related but nonpathogenic Escherichia coli strain expressing LPS of the O8 serotype was also examined. IcsA surface presentation in both of these genetic backgrounds continued to be unipolar, demonstrating that virulence plasmid-borne determinants are not responsible for unipolar localization of IcsA. The unipolar localization of IcsA in the E. coli background suggests that a common pathway that allows IcsA to be spatially restricted to one pole on the bacterial cell surface exists in Shigellaand E. coli.
机译：在感染的真核细胞中肌动蛋白尾巴和突起的有效形成需要志贺氏菌表面上IcsA的单极定位。脂多糖（LPS）突变已被证明会影响单极位置IcsA的建立或维持，尽管其机制尚不清楚。为了分析毒性质粒决定簇对IcsA的单极定位的贡献，我们在两个不同的遗传背景下检查了从克隆质粒拷贝表达的IcsA的定位。首先在野生型emS的毒力质粒固化的衍生物中检查IcsA的定位。 flexneri 2a分离株2457T。该方法检查了毒性质粒携带因子的作用，包括先前鉴定的毒性质粒携带蛋白酶，该蛋白酶负责在外膜中裂解IcsA并从细胞表面释放95 kDa分泌形式。 IcsA在相关但非致病性的表达O8血清型LPS的大肠杆菌中的定位也进行了检查。在这两个遗传背景下，IcsA表面的表现都仍然是单极性的，这表明毒力质粒携带的决定簇与IcsA的单极性定位无关。 IcsA在 E中的单极定位。大肠菌的背景表明，志贺氏菌和 E中存在一条共同途径，该途径可将IcsA在空间上限制在细菌细胞表面的一个极点上。大肠杆菌。

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