Spectral and sequence similarity between vasoactive intestinal peptide and the second conserved region of human immunodeficiency virus type 1 envelope glycoprotein (gp120): possible consequences on prevention and therapy of AIDS

Biochem Biophys Res Commun. 1992 Dec 15;189(2):705-10. doi: 10.1016/0006-291x(92)92258-y.


Recently, in sera of HIV infected individuals, antibodies recognizing nonimmunogenic C-terminal domain of the second conserved region of HIV-1 gp120 were identified (1). These antibodies are significantly more prevalent in asymptomatic carriers than in AIDS patients (1). Here we reported striking spectral and sequence homologies between human vasoactive intestinal peptide (VIP) and the conserved peptide derived from HIV-1 gp120 which binds these antibodies. The possible consequences of these findings on therapy and prevention of AIDS are discussed.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acquired Immunodeficiency Syndrome / blood
  • Acquired Immunodeficiency Syndrome / drug therapy*
  • Acquired Immunodeficiency Syndrome / prevention & control*
  • Amino Acid Sequence
  • Databases, Factual
  • HIV Antibodies / blood
  • HIV Envelope Protein gp120 / chemistry*
  • HIV-1 / genetics*
  • Humans
  • Molecular Sequence Data
  • Sequence Homology, Amino Acid
  • Spectrum Analysis
  • Vasoactive Intestinal Peptide / chemistry*


  • HIV Antibodies
  • HIV Envelope Protein gp120
  • Vasoactive Intestinal Peptide