Importance of the N-glycan in the V3 loop of HIV-1 envelope protein for CXCR-4- but not CCR-5-dependent fusion

FEBS Lett. 1998 Apr 24;426(3):367-72. doi: 10.1016/s0014-5793(98)00375-5.

Abstract

The V3 region of HIV-1 envelope protein possesses a single N-linked sugar chain, which is conserved in most HIV-1 strains. We studied its role in the life cycle of HIV-1 strains with different co-receptor usage. Removal of the glycan appeared to cause a marked reduction of CXCR-4- but not CCR-5-dependent virus entry. A basic amino acid substitution at the 11th position of V3 markedly compensated for the removal of the N-glycan. These results indicate that the N-glycan plays an important role for CXCR-4-dependent virus entry and that this role is exerted in a particular context of the peptide backbone.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Amino Acid Substitution
  • Cell Line, Transformed
  • Giant Cells / virology*
  • Glycosylation
  • HIV Envelope Protein gp120 / genetics
  • HIV Envelope Protein gp120 / metabolism*
  • HIV-1 / isolation & purification
  • HIV-1 / metabolism*
  • HIV-1 / physiology
  • Humans
  • Molecular Sequence Data
  • Mutagenesis, Site-Directed
  • Peptide Fragments / genetics
  • Peptide Fragments / metabolism*
  • Polysaccharides / physiology*
  • Receptors, CCR5 / physiology*
  • Receptors, CXCR4 / physiology*
  • Receptors, HIV / physiology
  • Virus Replication

Substances

  • HIV Envelope Protein gp120
  • HIV envelope protein gp120 (305-321)
  • Peptide Fragments
  • Polysaccharides
  • Receptors, CCR5
  • Receptors, CXCR4
  • Receptors, HIV