Yoshida K, Ohashi S, Kubo T, Tsuda T
Laboratory of Clinical Virology, Kyushu Research Station, National Institute of Animal Health, 2702, Chuzan, Kagoshima 891-0105, Japan.
J Clin Microbiol. 2000 Nov;38(11):4211-4. doi: 10.1128/JCM.38.11.4211-4214.2000.
Neutralizing monoclonal antibodies (MAbs) against the Aino virus were prepared, and the neutralizing epitopes of the virus were defined by competitive binding assay. Seven continuous and overlapping neutralizing epitopes existed on the G1 glycoprotein of the Aino virus. Two antigenic domains were identified and were designated I and II, with domain II consisting of six epitopes. Dot immunobinding assays (DIAs) were performed with MAbs that recognized these seven neutralizing epitopes. DIAs were performed with 1 Australian strain and 21 isolates found in Japan between the years 1964 and 1995. The MAb response patterns of all isolates were divided into four groups. The Japanese isolates did not show large differences in antigenicity, but the antigenicity of the Australian strain collected in 1968 was significantly different from that of the Japanese strains; the Australian strain lacked reactivity to three epitopes and showed only low reactivity to one epitope.
制备了抗爱诺病毒的中和单克隆抗体（MAb），并通过竞争结合试验确定了该病毒的中和表位。在爱诺病毒的G1糖蛋白上存在7个连续且重叠的中和表位。鉴定出两个抗原结构域，分别命名为I和II，其中结构域II由6个表位组成。用识别这7个中和表位的单克隆抗体进行斑点免疫结合试验（DIA）。对1株澳大利亚毒株和1964年至1995年间在日本发现的21株分离株进行了DIA试验。所有分离株的单克隆抗体反应模式分为4组。日本分离株在抗原性上没有显示出很大差异，但1968年收集的澳大利亚毒株的抗原性与日本毒株有显著差异；该澳大利亚毒株对3个表位无反应，对1个表位仅显示低反应性。
