Role of the S-typhimurium actin-binding protein SipA in bacterial internalization
Role of the S-typhimurium actin-binding protein SipA in bacterial internalization
复制标题
DOI：
10.1126/science.283.5410.2092
复制
发表时间：
1999-03-26
期刊：
影响因子：
56.9
通讯作者：
Galán, JE
中科院分区：
文献类型：
--
作者：
Zhou, D;Mooseker, MS;Galán, JE
鼠伤寒沙门氏菌进入宿主细胞需要细胞膜褶皱和肌动蛋白细胞骨架的重排。在这里，它表明细菌蛋白SipA在这个过程中起着关键作用。SiPA直接与肌动蛋白结合，降低其临界浓度，并抑制肌动蛋白丝的解聚，这些活性导致沙门氏菌诱导的膜皱褶的空间定位和更明显的向外延伸，从而促进细菌摄取。
Entry of the bacterium Salmonella typhimurium into host cells, requires membrane ruffling and rearrangement of the actin cytoskeleton. Here, it is shown that the bacterial protein SipA plays a critical role in this process. SipA binds directly to actin, decreases its critical concentration, and inhibits depolymerization of actin filaments, These activities result in the spatial localization and more pronounced outward extension of the Salmonella-induced membrane ruffles, thereby facilitating bacterial uptake.