Lafon M, Wiktor T J, Macfarlan R I
J Gen Virol. 1983 Apr;64 (Pt 4):843-51. doi: 10.1099/0022-1317-64-4-843.
Antigenic variation in the glycoprotein of rabies (CVS-11) virus was studied. Neutralization-resistant variant viruses were isolated in vitro at high frequency (10(-4) to 10(-5)) in the presence of anti-glycoprotein monoclonal antibody. Analysis of these variants identified at least three functionally independent antigenic sites, based on the grouping of variants that were no longer neutralized by one or more of a panel of 24 monoclonal antibodies. Competition radioimmunoassay suggested that one of these three antigenic sites was topologically distinct, with the other two in close proximity. In addition, it was shown that most (but not all) neutralization-resistant variants failed to bind the relevant monoclonal antibody. Viruses with altered antigenicity were shown to accumulate in virus stocks following several passages in vitro in the absence of antibody. In addition, variants were isolated in vivo following treatment of mice with monoclonal antibody.
对狂犬病（CVS - 11）病毒糖蛋白的抗原变异进行了研究。在抗糖蛋白单克隆抗体存在的情况下，体外以高频率（10^(-4)至10^(-5)）分离出抗中和变异病毒。基于一组24种单克隆抗体中的一种或多种不再能中和的变异株分组，对这些变异株的分析确定了至少三个功能独立的抗原位点。竞争放射免疫分析表明，这三个抗原位点之一在拓扑结构上是不同的，另外两个彼此靠近。此外，研究表明大多数（但不是全部）抗中和变异株无法结合相关单克隆抗体。在体外无抗体情况下传代几次后，抗原性改变的病毒在病毒储备液中积累。此外，在用单克隆抗体处理小鼠后，体内也分离出了变异株。
