针对可溶性CD4-rgp120复合物产生的抗体可识别CD4部分，并阻断膜融合，而不抑制CD4与gp120的结合。
Antibody raised against soluble CD4-rgp120 complex recognizes the CD4 moiety and blocks membrane fusion without inhibiting CD4-gp120 binding.
作者信息
Celada F, Cambiaggi C, Maccari J, Burastero S, Gregory T, Patzer E, Porter J, McDanal C, Matthews T
机构信息
Institute for Molecular Immunology, Hospital for Joint Disease, New York, New York.
出版信息
J Exp Med. 1990 Oct 1;172(4):1143-50. doi: 10.1084/jem.172.4.1143.
Abstract
We studied the humoral response of mice immunized with soluble CD4-rgp120 complex, testing polyclonal and monoclonal antibodies (mAbs) with the aim of identifying molecular changes that take place after the first interaction between human immunodeficiency virus and the cell surface. The antisera had a paradoxically high syncytia-blocking titer associated with anti-CD4 specificity, while their capacity to inhibit CD4-gp120 binding was relatively modest. One of the mAbs produced from these responders blocks syncytia formation but does not inhibit CD4 interaction with gp120. Apparently, this mAb interacts with the CD4 moiety of CD4-gp120 complex and prevents a post-binding event necessary for membrane fusion and viral infection.
摘要
我们研究了用可溶性CD4-rgp120复合物免疫的小鼠的体液反应，检测多克隆和单克隆抗体（mAb），目的是确定人类免疫缺陷病毒与细胞表面首次相互作用后发生的分子变化。抗血清具有与抗CD4特异性相关的异常高的细胞融合阻断效价，而它们抑制CD4-gp120结合的能力相对较弱。从这些反应者中产生的一种mAb可阻断细胞融合形成，但不抑制CD4与gp120的相互作用。显然，这种mAb与CD4-gp120复合物的CD4部分相互作用，并阻止膜融合和病毒感染所需的结合后事件。
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