Belaaouaj A, Kim K S, Shapiro S D
Department of Pediatrics, Washington University School of Medicine, St. Louis, MO 63110, USA.
Science. 2000 Aug 18;289(5482):1185-8. doi: 10.1126/science.289.5482.1185.
In determining the mechanism of neutrophil elastase (NE)-mediated killing of Escherichia coli, we found that NE degraded outer membrane protein A (OmpA), localized on the surface of Gram-negative bacteria. NE killed wild-type, but not OmpA-deficient, E. coli. Also, whereas NE-deficient mice had impaired survival in response to E. coli sepsis, as compared to wild-type mice, the presence or absence of NE had no influence on survival in response to sepsis that had been induced with OmpA-deficient E. coli. These findings define a mechanism of nonoxidative bacterial killing by NE and point to OmpA as a bacterial target in host defense.
在确定中性粒细胞弹性蛋白酶(NE)介导的大肠杆菌杀伤机制时,我们发现NE可降解位于革兰氏阴性菌表面的外膜蛋白A(OmpA)。NE可杀死野生型大肠杆菌,但不能杀死缺乏OmpA的大肠杆菌。此外,与野生型小鼠相比,缺乏NE的小鼠在应对大肠杆菌败血症时生存能力受损,而NE的存在与否对由缺乏OmpA的大肠杆菌诱导的败血症的生存情况没有影响。这些发现确定了NE非氧化杀伤细菌的机制,并指出OmpA是宿主防御中的细菌靶点。