Crawford L, Leppard K, Lane D, Harlow E
J Virol. 1982 May;42(2):612-20. doi: 10.1128/JVI.42.2.612-620.1982.
Several recently isolated monoclonal antibodies which reacted with simian virus 40 T antigens also reacted with proteins found in uninfected and untransformed cells. The proteins were different from each other, PAb419 reacting with a 35,000-molecular-weight protein, PAb427 reacting with a 75,000-molecular-weight phosphoprotein, PAb405 reacting with a 150,000-molecular-weight phosphoprotein, and PAb204 reacting with a 68,000-molecular-weight protein. It is suggested that although some of these cross-reactions may be fortuitous, they may, as an alternative, reflect similarities of shape and perhaps function between domains of the viral T antigen and the relevant host proteins.
几种最近分离出的与猴病毒40 T抗原发生反应的单克隆抗体,也与未感染和未转化细胞中发现的蛋白质发生反应。这些蛋白质彼此不同,PAb419与一种分子量为35,000的蛋白质发生反应,PAb427与一种分子量为75,000的磷蛋白发生反应,PAb405与一种分子量为150,000的磷蛋白发生反应,PAb204与一种分子量为68,000的蛋白质发生反应。有人提出,尽管其中一些交叉反应可能是偶然的,但它们也可能反映了病毒T抗原结构域与相关宿主蛋白质在形状甚至功能上的相似性。