Samson A C, Willcocks M M, Routledge E G, Morgan L A, Toms G L
J Gen Virol. 1986 Jul;67 ( Pt 7):1479-83. doi: 10.1099/0022-1317-67-7-1479.
A virus-neutralizing monoclonal antibody (1E3) specifically immunoprecipitated the 70000 mol. wt. (70K) fusion (F) protein from respiratory syncytial (RS) virus-infected HeLa cells. Western blotting analysis of polypeptides from such cells separated by SDS-polyacrylamide gel electrophoresis (SDS-PAGE) under reducing conditions revealed that 1E3 was peculiar in that it bound to both F1 (50K) and F2 (20K) components of the F protein. Antibody subsequently eluted from either the F1 or the F2 regions of immunoblots re-bound to both F1 and F2 regions of the SDS-PAGE blot. These results show that monoclonal antibody 1E3 reacts with an epitope which is found on both F1 and F2 subunits of RS virus fusion protein.
一种病毒中和单克隆抗体(1E3)能特异性地从呼吸道合胞病毒(RS)感染的HeLa细胞中免疫沉淀出分子量为70000道尔顿(70K)的融合(F)蛋白。在还原条件下,对经十二烷基硫酸钠 - 聚丙烯酰胺凝胶电泳(SDS - PAGE)分离的此类细胞的多肽进行蛋白质印迹分析表明,1E3的独特之处在于它能与F蛋白的F1(50K)和F2(20K)组分结合。随后从免疫印迹的F1或F2区域洗脱的抗体重新与SDS - PAGE印迹的F1和F2区域结合。这些结果表明,单克隆抗体1E3与呼吸道合胞病毒融合蛋白的F1和F2亚基上均存在的一个表位发生反应。