Weiss R A, Clapham P R, McClure M O, McKeating J A, McKnight A, Dalgleish A G, Sattentau Q J, Weber J N
Institute of Cancer Research, Chester Beatty Laboratories, London, U.K.
J Acquir Immune Defic Syndr (1988). 1988;1(6):536-41.
The envelope glycoproteins of HIV, gp120 and gp41, contain epitopes recognized by neutralizing antibodies. Studies of human sera from infected individuals indicate that group-specific neutralization antigens common to most isolates of HIV-1 exist, and that some HIV-2 antisera cross-neutralize HIV-1. Neutralization epitopes for HIV-1 have been identified and mapped, including a group-specific antigen on gp41, and a type-specific antigen on gp120. Neutralization "escape" mutants have been selected in vitro with a neutralizing mab to the type-specific antigenic loop. The CD4 antigen binds HIV-1 gp120 with high affinity and acts as the receptor on human and simian T-lymphocytes and monocytes for all strains of HIV-1, HIV-2, and SIV tested. Following binding to the CD4 receptor, HIV becomes internalized by a pH-independent process. The principle binding domain for gp120 is located in the N-terminal V domain of CD4. Anti-idiotypic sera to CD4 mabs recognizing the same site weakly neutralize HIVs of many strains, and soluble, recombinant forms of CD4 strongly neutralize HIV. Neither anti-CD4 mabs nor sCD4 inhibit the low level of plating of HIV observed on tumour cells in culture of glial (brain) and muscle origin, indicating that CD4 is not essential for infection of these cell types.
人类免疫缺陷病毒（HIV）的包膜糖蛋白gp120和gp41含有可被中和抗体识别的表位。对受感染个体的人血清研究表明，存在大多数HIV-1分离株共有的群特异性中和抗原，并且一些HIV-2抗血清可交叉中和HIV-1。已鉴定并绘制了HIV-1的中和表位，包括gp41上的群特异性抗原和gp120上的型特异性抗原。已用针对型特异性抗原环的中和单克隆抗体在体外筛选出中和“逃逸”突变体。CD4抗原以高亲和力结合HIV-1 gp120，并作为所有测试的HIV-1、HIV-2和猴免疫缺陷病毒（SIV）毒株在人和猴T淋巴细胞及单核细胞上的受体。与CD4受体结合后，HIV通过不依赖pH的过程内化。gp120的主要结合域位于CD4的N端V结构域。针对识别相同位点的CD4单克隆抗体的抗独特型血清可微弱中和许多毒株的HIV，而可溶性重组形式的CD4可强烈中和HIV。抗CD4单克隆抗体和可溶性CD4（sCD4）均不抑制在神经胶质（脑）和肌肉来源的肿瘤细胞培养物中观察到的HIV低水平接种，这表明CD4对于这些细胞类型的感染并非必不可少。
