Lipopolysaccharide remodeling in bacterial adaptation to host

由外膜酶LpxR脱酰的脂质A比未修饰的脂质A活性低，但比从LpxM突变体纯化的脂质A前体活性高。这些结果表明LpxR修饰脂质A有利于细菌适应宿主。coliW3110，并对脂质A的结构和蛋白组成进行了分析。 未观察到特异性脂质A修饰。另一方面，揭示了外膜囊泡含有鞭毛的组分鞭毛蛋白。 鞭毛形成的能力，包括鞭毛蛋白的合成，影响外膜囊泡的产生。

Lipid A deacylated by outer membrane enzyme LpxR is less active than unmodified lipid A, but more active than lipid A precursor purified from LpxM mutant. These results suggest that lipid A modification by LpxR is beneficial for bacterial adaptation to host.Outer membrane vesicle was prepared from E. coli W3110, and the structure of lipid A and its protein composition were examined. Specific lipid A modification was not observed. On the other hand, it was revealed that the outer membrane vescicle contained flagellin, a component of flagella. The ability to form flagella, including the synthesis of flagella proteins, affected the production of outer membrane vesicles.