Xue W, Orten D J, Abdelmagid O Y, Rider M, Blecha F, Minocha H C
Department of Laboratory Medicine, Kansas State University, Manhattan 66506.
Vet Microbiol. 1991 Nov;29(3-4):201-12. doi: 10.1016/0378-1135(91)90128-3.
Polyclonal rabbit anti-idiotypic antibodies (anti-ids) against two neutralizing murine monoclonal antibodies (mAbs) specific to a bovine viral diarrhea virus (BVDV) glycoprotein, 53 kDa, were produced, purified, and characterized. Each anti-id inhibited the binding of its respective mAb to BVDV antigen in a competitive ELISA and blocked the immunoprecipitation of the 53 kDa protein by the mAb. The anti-ids also inhibited the virus-neutralizing activity of their homologous mAbs. These results suggest that the anti-ids bear an internal image of a BVDV antigen and mimic neutralizing epitopes on the 53 kDa protein. Treatment of MDBK cells with the anti-ids inhibited BVDV infection, indicating that they block a cellular component, such as a virus receptor, required for virus adsorption or entry. Inhibition of the homologous mAb and lack of inhibition of the heterologous mAb indicate that the anti-ids are specific for the unique antigen-binding sites on the mAbs.
制备、纯化并鉴定了针对两种特异性识别牛病毒性腹泻病毒（BVDV）53 kDa糖蛋白的中和性鼠单克隆抗体（mAb）的多克隆兔抗独特型抗体（抗-ids）。在竞争性酶联免疫吸附测定（ELISA）中，每种抗-ids均抑制其相应mAb与BVDV抗原的结合，并阻断mAb对53 kDa蛋白的免疫沉淀。抗-ids还抑制其同源mAb的病毒中和活性。这些结果表明，抗-ids具有BVDV抗原的内影像，并模拟了53 kDa蛋白上的中和表位。用抗-ids处理牛肾传代细胞（MDBK细胞）可抑制BVDV感染，这表明它们阻断了病毒吸附或进入所需的细胞成分，如病毒受体。同源mAb受到抑制而异源mAb未受抑制，这表明抗-ids对mAb上独特的抗原结合位点具有特异性。
