Vordermeier H M, Hoffmann P, Gombert F O, Jung G, Bessler W G
Institut für Immunobiologie der Universität, Freiburg, Federal Republic of Germany.
Infect Immun. 1990 Aug;58(8):2719-24. doi: 10.1128/iai.58.8.2719-2724.1990.
After characterization of the porin OmpF and selection of molecular structures responsible for leukocyte activation by using computer-assisted epitope analysis, the analogs OmpF (153-174) (containing amino acids 153 to 174), OmpF (157-174), and OmpF (275-285) were synthesized and tested. Like the native protein, the segments were mitogenic for BALB/c splenocytes and induced B lymphocyte differentiation into antibody-producing plasma cells and tumor cytotoxicity of macrophages against the fibroblast cell line L929. We thus demonstrated that defined peptide segments are responsible for the leukocyte-activating properties of a major bacterial surface protein.
在对孔蛋白OmpF进行表征并通过计算机辅助表位分析选择负责白细胞激活的分子结构后,合成并测试了类似物OmpF(153 - 174)(包含氨基酸153至174)、OmpF(157 - 174)和OmpF(275 - 285)。与天然蛋白质一样,这些片段对BALB/c脾细胞具有促有丝分裂作用,并诱导B淋巴细胞分化为产生抗体的浆细胞,以及巨噬细胞对成纤维细胞系L929的肿瘤细胞毒性。因此,我们证明了特定的肽段负责一种主要细菌表面蛋白的白细胞激活特性。