Proteolytic Processing of the Human Immunodeficiency Virus Envelope Glycoprotein Precursor Decreases Conformational Flexibility

J Virol. 2013 Feb;87(3):1884-9. doi: 10.1128/JVI.02765-12. Epub 2012 Nov 21.

Abstract

The mature envelope glycoprotein (Env) spike on the surface of human immunodeficiency virus type 1 (HIV-1) virions is derived by proteolytic cleavage of a trimeric gp160 glycoprotein precursor. Remarkably, proteolytic processing of the HIV-1 Env precursor results in changes in Env antigenicity that resemble those associated with glutaraldehyde fixation. Apparently, proteolytic processing of the HIV-1 Env precursor decreases conformational flexibility of the Env trimeric complex, differentially affecting the integrity/accessibility of epitopes for neutralizing and nonneutralizing antibodies.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antibodies, Neutralizing / immunology
  • Antigens, Viral / chemistry*
  • Antigens, Viral / immunology
  • Antigens, Viral / metabolism*
  • Epitopes / immunology
  • HIV Antibodies / immunology
  • HIV Envelope Protein gp160 / chemistry*
  • HIV Envelope Protein gp160 / immunology
  • HIV Envelope Protein gp160 / metabolism*
  • Humans
  • Protein Conformation
  • Protein Processing, Post-Translational*
  • Proteolysis

Substances

  • Antibodies, Neutralizing
  • Antigens, Viral
  • Epitopes
  • HIV Antibodies
  • HIV Envelope Protein gp160
  • gp160 protein, Human immunodeficiency virus 1