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为获得对狂犬病病毒弱毒疫苗株筛选和糖蛋白抗原结构分析的单克隆抗体，将鹿狂犬病病毒 ８２０２ 株在适宜的条件下培养 ７２ ｈ，收集无细胞上清，经离心沉淀、 Ｚｎ （ Ａ Ｃ）２ 浓缩、１０％ ～５０％ 质量浓度的蔗糖密度梯度离心纯化、 Ｓ Ｄ Ｓ Ｐ Ａ Ｇ Ｅ 分析证明，产物中富含狂犬病病毒特异的结构蛋白。以上述纯化病毒免疫 Ｂ Ａ Ｌ Ｂ／ｃ 小鼠的脾细胞与 Ｓ Ｐ２／０ 骨髓瘤细胞融合，经 ３～５ 次克隆，间接 Ｅ Ｌ Ｉ Ｓ Ａ 筛选， Ｗ ｅｓｔｅｒｎ ｂｌｏｔｔｉｎｇ 鉴定，并与不同科病毒反应，建立了 ２ 株（４ Ａ５ ，３ Ａ５ ）可稳定分泌抗狂犬病病毒 Ｇ 蛋白的杂交瘤细胞株。这 ２ 株 Ｍ ｃ Ａｂ 与 ４株狂犬病病毒反应，经间接 Ｅ Ｌ Ｉ Ｓ Ａ 检测，发现能与强毒株反应，而与弱毒株不反应。细胞中和试验证实，这 ２株 Ｍ ｃ Ａｂ 具有良好的细胞中和活力。
To obtain a monoclonal antibody against rabies virus attenuated vaccine strain and glycoprotein antigen structure analysis, the rabies virus 8202 strain was cultured for 72 h under appropriate conditions. Cell-free supernatant was harvested, centrifuged, Zn (A C) 2 concentration, 10% ~ 50% concentration of sucrose density gradient centrifugation, SDS-PAGE analysis showed that the product is rich in rabies virus-specific structural proteins. The spleen cells of B A L B / c mice immunized with the above-mentioned purified virus were fused with S P2 / 0 myeloma cells, cloned 3 to 5 times, screened by indirect ELISA, and identified by Western blotting. Two strains (4 A5, 3 A5) of hybridoma cell lines stably secreting anti-rabies G protein were established. The two M c Abs reacted with four strains of rabies virus and were detected by indirect ELISA. They found that they reacted with virulent strains and did not react with attenuated strains. The cell neutralization assay confirmed that these two M c Abs had good cell-neutralizing activity.