Sokol P A, Woods D E
Infect Immun. 1986 Mar;51(3):896-900. doi: 10.1128/iai.51.3.896-900.1986.
An outer membrane protein of Pseudomonas aeruginosa was previously shown to bind 59Fe-labeled pyochelin. Antibodies to the purified ferripyochelin-binding protein (FBP) were characterized by using a variety of assays. Anti-FBP cross-reacted with several P. aeruginosa isolates in an enzyme-linked immunosorbent assay. Anti-FBP significantly enhanced phagocytosis of P. aeruginosa by human polymorphonuclear leukocytes. In a serum bactericidal assay we observed no difference in viability between cells incubated with antiserum to FBP and cells incubated with preimmune serum. Anti-FBP immunoglobulin G inhibited both binding and uptake of 59Fe-labeled pyochelin by whole cells. Passive protection by anti-FBP was examined in experimental P. aeruginosa burn infections in mice. The protection provided by this antibody was strain dependent but lipopolysaccharide serotype independent.
先前已表明铜绿假单胞菌的一种外膜蛋白能结合59Fe标记的绿脓菌素。通过多种检测方法对纯化的铁绿脓菌素结合蛋白(FBP)的抗体进行了表征。在酶联免疫吸附测定中,抗FBP与几种铜绿假单胞菌分离株发生交叉反应。抗FBP显著增强了人多形核白细胞对铜绿假单胞菌的吞噬作用。在血清杀菌试验中,我们观察到用抗FBP抗血清孵育的细胞与用免疫前血清孵育的细胞在活力上没有差异。抗FBP免疫球蛋白G抑制了全细胞对59Fe标记的绿脓菌素的结合和摄取。在小鼠铜绿假单胞菌烧伤感染实验中检测了抗FBP的被动保护作用。该抗体提供的保护作用具有菌株依赖性,但与脂多糖血清型无关。