Braun G, Cole S T
Mol Gen Genet. 1984;195(1-2):321-8. doi: 10.1007/BF00332766.
The cloned ompA gene from Serratia marcescens was fully expressed in Escherichia coli and its product correctly assembled into the outer membrane. The S. marcescens polypeptide was not functionally equivalent to the E. coli OmpA protein, which serves as a phage receptor and as a component of several colicin uptake systems. DNA sequence analysis of the gene showed that three regions of the protein likely to be exposed on the cell surface not only differed extensively from the corresponding regions of the E. coli polypeptide but also from all other sequenced OmpA proteins. It is suggested that this sequence polymorphism represents a safety mechanism by which the various enterobacterial species can avoid cross-infection by noxious agents such as phages or colicins.
从粘质沙雷氏菌克隆的ompA基因在大肠杆菌中得到充分表达,其产物正确组装到外膜中。粘质沙雷氏菌的多肽在功能上与大肠杆菌的OmpA蛋白不等同,后者作为噬菌体受体和几种大肠杆菌素摄取系统的一个组成部分。对该基因的DNA序列分析表明,该蛋白可能暴露在细胞表面的三个区域不仅与大肠杆菌多肽的相应区域有很大差异,而且与所有其他已测序的OmpA蛋白也有很大差异。有人提出,这种序列多态性代表了一种安全机制,通过这种机制,各种肠杆菌科细菌可以避免被噬菌体或大肠杆菌素等有害物质交叉感染。