Acquisition of omptin reveals cryptic virulence function of autotransporter YapE in Yersinia pestis.
Acquisition of omptin reveals cryptic virulence function of autotransporter YapE in Yersinia pestis.
复制标题
获得 omptin 揭示了鼠疫耶尔森菌中自转运蛋白 YapE 的神秘毒力功能。
DOI：
10.1111/mmi.12273
复制
发表时间：
2013
影响因子：
3.6
通讯作者：
Miller,VirginiaL
中科院分区：
文献类型：
--
作者：
Lawrenz,MatthewB;Pennington,Jarrod;Miller,VirginiaL
自身转运蛋白是革兰氏阴性菌中最大的分泌蛋白家族，具有多种功能，包括粘附、细胞毒性和免疫逃避。在鼠疫耶尔森氏菌中，自转运蛋白YapE具有粘附特性，并在腺鼠疫小鼠模型中促成疾病。在这里，我们证明了鼠疫耶尔森菌YapE的omptin裂解是介导细菌聚集和粘附真核细胞所必需的。我们证明，omptin切割是鼠疫耶尔森菌和假结核耶尔森菌YapE直向同源物的特异性，但在小肠结肠炎耶尔森菌蛋白中不保守。我们还表明，YapE的切割发生在鼠疫耶尔森氏菌中，但不发生在肠道耶尔森氏菌种中，并且需要omptin Pla（纤溶酶原激活蛋白酶），该蛋白酶在鼠疫耶尔森氏菌特异性质粒pPCP 1上编码。总之，这些数据表明，YapE的翻译后修饰似乎对鼠疫耶尔森氏菌具有特异性，在鼠疫耶尔森氏菌与假结核耶尔森氏菌分化期间沿着pPCP 1的获得，并且是调节细菌粘附的新机制的第一个证据。
Autotransporters, the largest family of secreted proteins in Gram‐negative bacteria, perform a variety of functions, including adherence, cytotoxicity and immune evasion. InYersinia pestisthe autotransporter YapE has adhesive properties and contributes to disease in the mouse model of bubonic plague. Here, we demonstrate that omptin cleavage ofY. pestisYapE is required to mediate bacterial aggregation and adherence to eukaryotic cells. We demonstrate that omptin cleavage is specific for theY. pestisandY. pseudotuberculosisYapE orthologues but is not conserved in theYersinia enterocoliticaprotein. We also show that cleavage of YapE occurs inY. pestisbut not in the entericYersiniaspecies, and requires the omptin Pla (plasminogen activator protease), which is encoded on theY. pestis‐specific plasmid pPCP1. Together, these data show that post‐translation modification of YapE appears to be specific toY. pestis, was acquired along with the acquisition of pPCP1 during the divergence ofY. pestisfromY. pseudotuberculosis, and are the first evidence of a novel mechanism to regulate bacterial adherence.