Ruppert A, Arnold N, Hobom G
Institut für Mikrobiologie und Molekularbiologie, Justus Liebig-Universität Giessen, Germany.
Vaccine. 1994 May;12(6):492-8. doi: 10.1016/0264-410x(94)90305-0.
Exposure at the bacterial outer surface of the major antigenic epitope of the foot-and-mouth disease (FMDV) viral protein VP1 was studied using protein fusion with outer membrane protein A (OmpA) of Shigella dysenteriae for production and transport of the foreign polypeptide to the outer membrane of Escherichia coli. Fusion constructs with VP1 peptide insertions of up to 56 amino acids in the third outer domain of OmpA could be demonstrated on the bacterial surface by indirect immunofluorescence and immunogold labelling. OmpA fusion proteins with large insertions from sequences of the FMDV protein VP1 were shown to elicit virus-specific immune responses in rabbits.
利用与痢疾志贺氏菌外膜蛋白A(OmpA)的蛋白融合,将外来多肽生产并转运至大肠杆菌外膜,研究口蹄疫病毒(FMDV)病毒蛋白VP1主要抗原表位在细菌外表面的暴露情况。通过间接免疫荧光和免疫金标记可在细菌表面证实,在OmpA的第三个外部结构域插入多达56个氨基酸的VP1肽的融合构建体。含有来自FMDV蛋白VP1序列的大插入片段的OmpA融合蛋白在兔体内可引发病毒特异性免疫反应。