Relationships between the anti-HIV V(3)-derived peptide SPC(3) and lymphocyte membrane properties involved in virus entry: SPC(3) interferes with CXCR(4)

FEMS Microbiol Lett. 2000 Feb 15;183(2):235-40. doi: 10.1111/j.1574-6968.2000.tb08964.x.

Abstract

SPC(3) is a multiple antigen peptide derived from the V(3) loop of human immunodeficiency virus (HIV) envelope (Env). It exerts a potent anti-HIV activity whereas it alters neither Env expression nor binding to CD(4). Here, SPC(3) binding characteristics, its subsequent intracellular fate and the fact that it inhibited SDF(1)alpha binding to the lymphocyte surface provided strong arguments to conclude that it exerts its anti-HIV activity through interference with the CXCR(4) coreceptor. In contrast, it interferes with none of the other major surface proteins and mechanisms involving V(3) and implicated in infection, as shown here. This work identifies the target mechanism of SPC(3).

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Anti-HIV Agents / pharmacology*
  • Cell Line
  • Cell Membrane / metabolism
  • Cricetinae
  • Dipeptidyl Peptidase 4 / metabolism
  • HIV Envelope Protein gp120 / metabolism
  • HIV Envelope Protein gp120 / pharmacology*
  • Humans
  • Lymphocytes / drug effects*
  • Phosphorylation
  • Receptors, CXCR4 / drug effects
  • Receptors, CXCR4 / physiology*
  • Recombinant Proteins
  • Thrombin / pharmacology

Substances

  • Anti-HIV Agents
  • HIV Envelope Protein gp120
  • Receptors, CXCR4
  • Recombinant Proteins
  • SPC3 peptide
  • Dipeptidyl Peptidase 4
  • Thrombin