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YopM蛋白是致病性耶尔森菌的毒力因子之一 ,本文介绍了其结构、定位及功能等方面的研究进展。YopM蛋白是一个亮氨酸丰富区 (LRR)蛋白质家族的成员 ,其晶体结构提示它可作为蛋白质骨架与其他蛋白质相互作用。早期研究认为YopM可结合α 凝血酶 ,抑制凝血酶引起的血小板聚集。后来发现YopM CyaA融合蛋白可通过Ⅲ型分泌系统定向进入真核细胞。免疫荧光定位显示YopM不但可进入宿主细胞质 ,而且通过小泡相关通路进入细胞核。在哺乳动物细胞内 ,YopM与 2种靶物质PRK2和RSK1形成一种新的蛋白复合体 ,并激活PRK2和RSK1的激酶活性。YopM在耶尔森菌感染中的功能和致病机制有待进一步研究。
YopM protein is one of the virulence factors of pathogenic Yersinia. This paper introduces the research progress of its structure, localization and function. The YopM protein is a member of the leucine rich region (LRR) protein family whose crystal structure suggests that it can interact with other proteins as a protein backbone. Early studies suggest that YopM binds to alpha-thrombin and inhibits thrombin-induced platelet aggregation. It was later found that the YopM CyaA fusion protein can be targeted into eukaryotic cells via the type III secretion system. Immunofluorescence mapping showed that YopM not only entered the host cytoplasm, but also entered the nucleus through vesicle-associated pathways. In mammalian cells, YopM forms a new protein complex with the two target substances PRK2 and RSK1 and activates the kinase activity of PRK2 and RSK1. YopM Yersinia infection in the function and pathogenesis needs further study.