Lundin K, Nygren A, Arthur L O, Robey W G, Morein B, Ramstedt U, Gidlund M, Wigzell H
J Immunol Methods. 1987 Feb 26;97(1):93-100. doi: 10.1016/0022-1759(87)90110-4.
The HIV (HTLV-III) envelope glycoprotein, Gp120, was isolated from virus-infected tissue culture cells using affinity chromatography. A radioimmunoassay was developed to determine the degree of iodinated Gp120 to target CD4+ (T4+) cells. 125I-Gp120 could be shown to selectively bind to CD4+ cells only. The Gp120 remained bound to these cells after repeated washes. Monoclonal anti-CD4 antibodies block the binding of Gp120 to CD4+ cells. Monoclonal antibodies to other cell surface components do not interfere with 125I-Gp120 binding. All IgG antibodies from HIV seropositive donors tested block 125I-Gp120 binding, though with variable titers. We believe that this assay provides further proof for the use of CD4 (T4) as a component of the receptor for HIV. It represents a safe, objective and sensitive method for the analysis of Gp120-CD4 interactions, as well as the potential of antibodies to interfere with this binding.
使用亲和层析法从病毒感染的组织培养细胞中分离出HIV（HTLV-III）包膜糖蛋白Gp120。开发了一种放射免疫测定法来确定碘化Gp120靶向CD4 +（T4 +）细胞的程度。结果表明，125I-Gp120仅能选择性地与CD4 +细胞结合。反复洗涤后，Gp120仍与这些细胞结合。单克隆抗CD4抗体可阻断Gp120与CD4 +细胞的结合。针对其他细胞表面成分的单克隆抗体不会干扰125I-Gp120的结合。尽管效价不同，但所有来自HIV血清阳性供体的IgG抗体均能阻断125I-Gp120的结合。我们认为该测定法为将CD4（T4）用作HIV受体的组成部分提供了进一步的证据。它代表了一种安全、客观且灵敏的方法，可用于分析Gp120-CD4相互作用以及抗体干扰这种结合的可能性。
