Tommassen J, Vermeij P, Struyvé M, Benz R, Poolman J T
Department of Molecular Cell Biology, State University of Utrecht, The Netherlands.
Infect Immun. 1990 May;58(5):1355-9. doi: 10.1128/iai.58.5.1355-1359.1990.
The class 1 major outer membrane protein of Neisseria meningitidis is a serious candidate for a meningococcal vaccine. To facilitate studies on the function of this protein, mutants were isolated that lacked this protein or the structurally related class 3 protein. These mutants were obtained by using the antibody-dependent bactericidal action of the complement system. The class 1 protein-deficient strain grew normally in vitro, whereas growth of the class 3 protein-deficient strain was slightly retarded. The class 3 protein-deficient strain displayed increased resistance to the antibiotics tetracycline and cefsulodin, which is consistent with the proposed role of the protein as a pore-forming protein. The class 1 protein was purified to homogeneity from the class 3 protein-deficient strain. Lipid bilayer experiments revealed that this protein also formed pores. The class 1 protein pores were cation selective.
脑膜炎奈瑟菌的1类主要外膜蛋白是脑膜炎球菌疫苗的一个重要候选对象。为便于研究该蛋白的功能,分离出了缺乏这种蛋白或结构相关的3类蛋白的突变体。这些突变体是利用补体系统的抗体依赖性杀菌作用获得的。1类蛋白缺陷菌株在体外正常生长,而3类蛋白缺陷菌株的生长略有延迟。3类蛋白缺陷菌株对四环素和头孢磺啶抗生素的抗性增加,这与该蛋白作为成孔蛋白的推测作用一致。从3类蛋白缺陷菌株中纯化出了纯的1类蛋白。脂质双层实验表明该蛋白也形成孔。1类蛋白孔具有阳离子选择性。