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

✍ Scribed by L. H. Den Van Berg; S. A. Sadiq; S. Lederman; N. Latov

• Publisher: John Wiley and Sons
• Year: 1992
• Tongue: English
• Weight: 534 KB
• Volume: 33
• Category: Article
• ISSN: 0360-4012
• DOI: 10.1002/jnr.490330403

✦ Synopsis

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.