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HIV-1的糖蛋白120与硫苷脂和髓鞘相关糖蛋白结合。

The gp120 glycoprotein of HIV-1 binds to sulfatide and to the myelin associated glycoprotein.

作者信息

van den Berg L H, Sadiq S A, Lederman S, Latov N

机构信息

Department of Neurology, Columbia University, New York NY 10032.

出版信息

J Neurosci Res. 1992 Dec;33(4):513-8. doi: 10.1002/jnr.490330403.

DOI:10.1002/jnr.490330403
PMID:1282933
Abstract

We investigated the binding of the gp120 glycoprotein of the human immunodeficiency virus (HIV-1) to neural glycolipids and glycoproteins by ELISA. The gp120 protein bound to sulfatide (GalS), a sulfated glycolipid autoantigen implicated in sensory neuritis, and to the myelin associated glycoprotein (MAG), an autoantigen in demyelinating neuropathy. Binding of gp120 to MAG was inhibited by the HNK-1 antibody, which recognizes a sulfated glucuronic acid epitope, suggesting that the interaction involves carbohydrate determinants. Sulfatide and MAG are potential receptors for gp120 in peripheral nerve and may have a role in the neuropathy associated with HIV-1 infection.

摘要

我们通过酶联免疫吸附测定法(ELISA)研究了人类免疫缺陷病毒(HIV-1)的糖蛋白120(gp120)与神经糖脂及糖蛋白的结合情况。gp120蛋白可与硫苷脂(GalS)结合,硫苷脂是一种与感觉神经炎相关的硫酸化糖脂自身抗原,同时gp120蛋白也可与髓鞘相关糖蛋白(MAG)结合,MAG是脱髓鞘性神经病变中的一种自身抗原。gp120与MAG的结合可被识别硫酸化葡萄糖醛酸表位的HNK-1抗体所抑制,这表明这种相互作用涉及碳水化合物决定簇。硫苷脂和MAG可能是gp120在外周神经中的潜在受体,并且可能在与HIV-1感染相关的神经病变中发挥作用。

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