Moore J P, McKeating J A, Jones I M, Stephens P E, Clements G, Thomson S, Weiss R A
Chester Beatty Laboratories, Institute of Cancer Research, London, UK.
AIDS. 1990 Apr;4(4):307-15. doi: 10.1097/00002030-199004000-00004.
We compared four preparations of recombinant HIV-1 envelope glycoprotein: mammalian (Chinese hamster ovary cells) gp120 (Celltech); baculovirus gp120 from American Biotechnologies Inc. (ABT) and from MicroGeneSys (MGS); and baculovirus gp160 (Institute of Virology, Oxford, UK). Each envelope glycoprotein binds to a neutralizing monoclonal antibody (MAb) directed against the V3 loop, confirming the integrity of this type-specific neutralization epitope. MGS gp120 binds abnormally well to a MAb which recognizes an epitope preferentially exposed on denatured gp120. Consistent with this finding, MGS gp120 binds to soluble CD4 (sCD4) with an affinity 50-100-fold lower than that of Celltech gp120. The affinity of Celltech gp120 from sCD4 is 2.3 nM, indistinguishable from that of gp120 extracted from HIV-1 virions. Baculovirus gp120 (ABT) and gp160 also have a high affinity for sCD4. A significant proportion of anti-gp120 antibodies in HIV-positive human sera recognize epitopes that are dependent on the mammalian glycosylation pattern, and a human HIV-positive serum inhibits the binding of mammalian gp120 to sCD4 five- to 10-fold more potently than it inhibits baculovirus gp120 binding to sCD4.
我们比较了四种重组HIV-1包膜糖蛋白制剂：哺乳动物（中国仓鼠卵巢细胞）gp120（Celltech公司）；美国生物技术公司（ABT）和MicroGeneSys公司（MGS）的杆状病毒gp120；以及杆状病毒gp160（英国牛津病毒研究所）。每种包膜糖蛋白都能与一种针对V3环的中和单克隆抗体（MAb）结合，证实了这种型特异性中和表位的完整性。MGS gp120与一种识别优先暴露于变性gp120上的表位的单克隆抗体结合异常良好。与此发现一致的是，MGS gp120与可溶性CD4（sCD4）的结合亲和力比Celltech gp120低50至100倍。Celltech gp120与sCD4的亲和力为2.3 nM，与从HIV-1病毒粒子中提取的gp120的亲和力无差异。杆状病毒gp120（ABT）和gp160对sCD4也有高亲和力。HIV阳性人血清中相当一部分抗gp120抗体识别依赖于哺乳动物糖基化模式的表位，并且一份HIV阳性人血清抑制哺乳动物gp120与sCD4结合的效力比抑制杆状病毒gp120与sCD4结合的效力高5至10倍。
