Michiels T, Wattiau P, Brasseur R, Ruysschaert J M, Cornelis G
Unité de Microbiologie, Université Catholique de Louvain, Brussels, Belgium.
Infect Immun. 1990 Sep;58(9):2840-9. doi: 10.1128/iai.58.9.2840-2849.1990.
Upon incubation at 37 degrees C in the absence of Ca2+ ions, pathogenic strains of the genus Yersinia cease growing and produce large amounts of a series of plasmid-encoded proteins involved in pathogenicity. These proteins, called Yops (for Yersinia outer membrane proteins), are detected in both the outer membrane fraction and the culture supernatant. We present here the nucleotide sequence of genes yop20 and yop25 from Yersinia enterocolitica O:9. Protein Yop25 is very similar to YopE, the corresponding protein from Yersinia pestis, Y. pseudotuberculosis, and Y. enterocolitica O:8 (A. Forsberg and H. Wolf-Watz, J. Bacteriol. 172:1547-1555, 1990). This is the first report of a yop20 sequence of yersiniae. We present evidences that Yops are not membrane proteins. Their detection in the membrane fraction results either from copurification of large aggregates of extracellular Yops with the membrane fraction or from the adsorption of released proteins to the cell surface. In contrast with Yops, protein P1 has characteristics of a true membrane protein. The release of Yops by Y. enterocolitica occurs by a novel secretion mechanism that does not involve the cleavage of a typical signal sequence or the recognition of a carboxy-terminal domain.
在无钙离子存在的情况下于37摄氏度培养时，耶尔森氏菌属的致病菌株停止生长，并产生大量与致病性有关的一系列质粒编码蛋白。这些蛋白称为Yops（耶尔森氏菌外膜蛋白），在外膜组分和培养上清液中均能检测到。我们在此展示了来自小肠结肠炎耶尔森氏菌O:9的yop20和yop25基因的核苷酸序列。蛋白Yop25与来自鼠疫耶尔森氏菌、假结核耶尔森氏菌和小肠结肠炎耶尔森氏菌O:8的相应蛋白YopE非常相似（A. 福斯贝里和H. 沃尔夫 - 瓦茨，《细菌学杂志》172:1547 - 1555，1990年）。这是关于耶尔森氏菌yop20序列的首次报道。我们提供证据表明Yops不是膜蛋白。它们在膜组分中的检测要么是由于细胞外Yops的大聚集体与膜组分共纯化，要么是由于释放的蛋白吸附到细胞表面。与Yops不同，蛋白P1具有真正膜蛋白的特征。小肠结肠炎耶尔森氏菌释放Yops是通过一种新的分泌机制，该机制不涉及典型信号序列的切割或羧基末端结构域的识别。
