Binding of HIV-1 gp120 to the nicotinic receptor

FEBS Lett. 1992 Oct 19;311(2):115-8. doi: 10.1016/0014-5793(92)81380-5.

Abstract

We previously described a significant sequence homology between HIV-1 gp120 and the functional sites responsible for the specific binding of snake curare-mimetic neurotoxins and rabies virus glycoprotein to the nicotinic acetylcholine receptor. Here we report findings about the existence of a mechanism of functional molecular mimicry which could enable the binding of HIV-1 gp120 to nicotinic acetylcholine receptors in muscle cells and neurons.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylcholine / pharmacology
  • Amino Acid Sequence
  • Antigens, Viral*
  • Binding, Competitive
  • Bungarotoxins / metabolism
  • Glycoproteins / chemistry
  • HIV Envelope Protein gp120 / chemistry
  • HIV Envelope Protein gp120 / metabolism*
  • HIV Envelope Protein gp120 / pharmacology
  • HIV-1 / metabolism*
  • Humans
  • Molecular Sequence Data
  • Muscles / metabolism
  • Neurotoxins / chemistry
  • Nicotine / pharmacology
  • Receptors, Nicotinic / metabolism*
  • Sequence Homology, Amino Acid
  • Tumor Cells, Cultured
  • Viral Envelope Proteins / chemistry

Substances

  • Antigens, Viral
  • Bungarotoxins
  • Glycoproteins
  • HIV Envelope Protein gp120
  • Neurotoxins
  • Receptors, Nicotinic
  • Viral Envelope Proteins
  • glycoprotein G, Rabies virus
  • Nicotine
  • Acetylcholine