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

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


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.

MeSH terms

  • Animals
  • Antibodies, Monoclonal
  • CD4 Antigens / metabolism
  • Enzyme-Linked Immunosorbent Assay
  • Glycolipids / metabolism*
  • HIV Envelope Protein gp120 / metabolism*
  • HIV-1 / metabolism*
  • Kinetics
  • Mice
  • Myelin Proteins / metabolism*
  • Myelin-Associated Glycoprotein
  • Protein Binding
  • Proteoglycans / metabolism*
  • Recombinant Proteins / metabolism
  • Sulfoglycosphingolipids / metabolism*


  • Antibodies, Monoclonal
  • CD4 Antigens
  • Glycolipids
  • HIV Envelope Protein gp120
  • Myelin Proteins
  • Myelin-Associated Glycoprotein
  • Proteoglycans
  • Recombinant Proteins
  • Sulfoglycosphingolipids