Navarro-Garcia Fernando, Sonnested Michael, Teter Ken
Department of Cell Biology, Centro de Investigación y de Estudios Avanzados del IPN (CINVESTAV-Zacatenco), Ap. Postal 14-740, 07000 México DF, Mexico;
Toxins (Basel). 2010 May 1;2(5):1134-1147. doi: 10.3390/toxins2051134.
EspC and Pet are toxins secreted by the diarrheagenic enteropathogenic and enteroaggregative Escherichia coli pathotypes, respectively. Both toxins have a molecular mass around 110 kDa and belong to the same protein family called Serine Protease Autotransporters of the Enterobacteriaceae (SPATE). Furthermore, both toxins act within the cytosol of intoxicated epithelial cells to disrupt the architecture of the actin cytoskeleton. This cytopathic and enterotoxic effect results from toxin cleavage of the actin-binding protein fodrin, although the two toxins recognize different cleavage sites on fodrin. EspC and Pet also have dramatically different mechanisms of entering the target cell which appear dependent upon the E. coli pathotype. In this review, we compare/contrast EspC and Pet in regards to their mode of delivery into the target cell, their effects on fodrin and the actin cytoskeleton, and their possible effects on the physiology of the intestinal epithelial cell.
EspC和Pet分别是由致泻性肠致病性大肠杆菌和肠集聚性大肠杆菌分泌的毒素。这两种毒素的分子量均约为110 kDa，属于同一蛋白质家族，称为肠杆菌科丝氨酸蛋白酶自转运体（SPATE）。此外，这两种毒素都在中毒上皮细胞的细胞质中起作用，破坏肌动蛋白细胞骨架的结构。这种细胞病变和肠毒素作用是由毒素切割肌动蛋白结合蛋白血影蛋白引起的，尽管这两种毒素识别血影蛋白上不同的切割位点。EspC和Pet进入靶细胞的机制也有很大不同，这似乎取决于大肠杆菌的致病类型。在这篇综述中，我们比较/对比了EspC和Pet在进入靶细胞的方式、它们对血影蛋白和肌动蛋白细胞骨架的影响以及它们对肠上皮细胞生理学可能产生的影响。
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