Liang C M, Henry S, Liang S M, Epstein J S
Center for Biologics Evaluation and Research, FDA, Bethesda, MD 20892.
J Immunol Methods. 1990 Aug 28;132(1):57-62. doi: 10.1016/0022-1759(90)90398-f.
We produced three murine monoclonal antibodies (mAbs) against the HIV-1 proteins. These three mAbs, namely CA-1, CA-2, CA-4, were IgG1 and all reacted with p24 on the HIV-1 Western blot. One of the mAbs, CA-4, also recognized p13, p21, p28, p29, p32, p39, p47, p55 on the Biotech/Du Pont HIV-1 Western blot strips and p21, p24, p28, p29, p39, p47, p55, p68, p80, p96; p110 on the Bio-Rad strips. CA-4 did not react with H-9 cell lysate nor with other retroviral antigens such as HTLV-1 or HIV-2 proteins. The binding of CA-4 to HIV-1 proteins was not blocked by deglycosylation. All three mAbs reacted with recombinant DNA derived capsid protein (p24) of HIV-1. These results suggest that many proteins in the HIV-1 Western blot contain antigenic epitope(s) similar to that of p24.
我们制备了三种针对HIV-1蛋白的鼠单克隆抗体（mAb）。这三种单克隆抗体，即CA-1、CA-2、CA-4，均为IgG1，且在HIV-1免疫印迹上均与p24发生反应。其中一种单克隆抗体CA-4，在Biotech/Du Pont HIV-1免疫印迹条带上还识别p13、p21、p28、p29、p32、p39、p47、p55，在Bio-Rad条带上识别p21、p24、p28、p29、p39、p47、p55、p68、p80、p96；p110。CA-4不与H-9细胞裂解物反应，也不与其他逆转录病毒抗原如HTLV-1或HIV-2蛋白反应。去糖基化不会阻断CA-4与HIV-1蛋白的结合。所有三种单克隆抗体均与HIV-1的重组DNA衍生衣壳蛋白（p24）反应。这些结果表明，HIV-1免疫印迹中的许多蛋白含有与p24相似的抗原表位。
