Cole S T, Sonntag I, Henning U
J Bacteriol. 1982 Jan;149(1):145-50. doi: 10.1128/jb.149.1.145-150.1982.
The outer membranes of many gram-negative bacteria contain a major heat-modifiable protein which shows serological cross-reactivity with the OmpA protein of Escherichia coli K-12. Using the cloned gene for the E. coli K12 protein as a DNA-DNA hybridization probe, we were able to identify the corresponding genes from Shigella dysenteriae. Enterobacter aerogenes, and Serratia marcescens. These were cloned in a phage lambda vector, and their expression in E. coli K-12 was studied. All three OmpA proteins were fully produced and correctly exported to the outer membrane. In several cases, complete or partial restoration of known function of the E. coli K-12 protein was observed.
许多革兰氏阴性菌的外膜含有一种主要的热可修饰蛋白,该蛋白与大肠杆菌K-12的OmpA蛋白表现出血清学交叉反应。利用克隆的大肠杆菌K12蛋白基因作为DNA-DNA杂交探针,我们能够从痢疾志贺氏菌、产气肠杆菌和粘质沙雷氏菌中鉴定出相应的基因。这些基因被克隆到λ噬菌体载体中,并研究了它们在大肠杆菌K-12中的表达。所有三种OmpA蛋白都能完全产生并正确转运到外膜。在几种情况下,观察到大肠杆菌K-12蛋白已知功能的完全或部分恢复。