大肠杆菌外膜蛋白酶T研究进展

Research Progress on Outer Membrane Protease T of Escherichia coli

外膜蛋白酶T(Outer membrane protease T,OmpT)是大肠杆菌外膜的一种蛋白水解酶,是Omptin家族中第一个被解析结构的外膜蛋白,由10条反向平行的β折叠构成中空的桶状结构。OmpT能够识别两个连续的碱性氨基酸,并水解鱼精蛋白和血纤维蛋白溶酶原等。脂多糖(Lipopolysaccharide,LPS)对OmpT蛋白酶功能的激活具有重要作用。研究发现,OmpT对细菌的定植和黏附至关重要。文章围绕OmpT的结构、功能、毒力等方面综述该蛋白当前的研究进展。

Outer membrane protease T(OmpT)is a proteolytic enzyme of Escherichia coli(E.coli)outer membrane,which is the first outer membrane protein of Omptin family to be resolved.Consisting of 10 antiparallelβ-sheets and a hollow barrel,OmpT can recognize two consecutive basic amino acids,hydrolyze protamine and plasminogen.LPS(Lipopolysaccharide)plays an important role in the activation of OmpT protease.Studies had found that OmpT was vital during bacterial colonization and adhesion to hosts.This article focused on the current research progress of OmpT,including corresponding structure,function,and virulence.