Merza M, Sundquist B, Söber J, Morein B
Department of Veterinary Microbiology, Swedish University of Agricultural Sciences, Uppsala.
J Virol Methods. 1991 Aug;33(3):345-53. doi: 10.1016/0166-0934(91)90034-w.
The outer envelope glycoprotein gp51 and the core protein p24 of bovine leukemia virus (BLV), were purified from culture media of FLK-BLV cells by a single-step procedure, using immunoaffinity chromatography based on monoclonal antibodies to the respective proteins. About 90% of the envelope glycoprotein in the culture medium was recovered as a highly purified product. Both purified protein (gp51 and p24) preparations, were found to be highly specific antigens by ELISA, and did not cross-react with sera raised against the other antigen. The conformational epitopes on the purified gp51 were preserved as judged by their reactions with the corresponding monoclonal antibodies. The p24 ELISA reacted only with sera from naturally infected animals and not with sera from animals immunized with an experimental gp51-iscom vaccine. The p24 antigen is therefore useful for discriminating between BLV-infected animals and those immunized with a gp51 subunit vaccine.
牛白血病病毒（BLV）的外膜糖蛋白gp51和核心蛋白p24，通过一步法从FLK - BLV细胞的培养基中纯化得到，该方法基于针对各自蛋白的单克隆抗体进行免疫亲和层析。培养基中约90%的包膜糖蛋白以高度纯化的产物形式回收。通过酶联免疫吸附测定（ELISA）发现，两种纯化的蛋白制剂（gp51和p24）都是高度特异性的抗原，并且不会与针对另一种抗原产生的血清发生交叉反应。通过与相应单克隆抗体的反应判断，纯化的gp51上的构象表位得以保留。p24 ELISA仅与自然感染动物的血清反应，而不与用实验性gp51 - 免疫刺激复合物疫苗免疫的动物血清反应。因此，p24抗原可用于区分感染BLV的动物和用gp51亚单位疫苗免疫的动物。
