Effect of polyanion-resistance on HIV-1 infection

Virology. 2004 Aug 1;325(2):389-98. doi: 10.1016/j.virol.2004.05.011.

Abstract

Polyanions are potent HIV-1 entry inhibitors. Nevertheless, resistant viruses may emerge under polyanion inhibitory pressure. Specifically, a polyanion-resistant virus replicates in T cells even in the presence of high concentrations of polyanions. We found that although the polyanion-resistant virus grows in suspension CD4+ T cells efficiently, it infects nonlymphocytic adherent CD4+ cells poorly. Given that a main distinction between suspension and adherent cells is the absence or presence of cell-surface heparan sulfate proteoglycan (HSPG), we investigated if the failure of the polyanion-resistant virus to infect adherent CD4+ cells arises from its inability to bind HSPG. We found that the emergence of mutations in gp120 associated with polyanion resistance resulted in a decreased capacity of HIV-1 to bind HSPG. We also found that the polycation polybrene rescued the capacity of the polyanion-resistant virus to bind HSPG and to infect adherent CD4+ cells. The identification of this virus, unable to bind HSPG, provides a convenient probe to measure the impact of HIV-1-HSPG interactions in vivo. Altogether, these findings suggest that polyanion-resistance narrows the range of potential target cells for HIV-1 in the host. This reinforces the hypothesis that cell-free or cell-associated polyanions such as HSPG possess the capacity to modulate HIV-1 pathogenesis.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Amino Acid Substitution
  • Anti-HIV Agents / pharmacology*
  • Binding Sites
  • CD4 Antigens / metabolism
  • CD4-Positive T-Lymphocytes / drug effects
  • CD4-Positive T-Lymphocytes / immunology
  • CD4-Positive T-Lymphocytes / metabolism
  • CD4-Positive T-Lymphocytes / virology
  • Cell Line
  • Drug Resistance, Viral / genetics
  • HIV Envelope Protein gp120 / chemistry
  • HIV Envelope Protein gp120 / genetics
  • HIV Infections / drug therapy
  • HIV Infections / virology
  • HIV-1 / drug effects*
  • HIV-1 / genetics
  • HIV-1 / pathogenicity
  • HIV-1 / physiology
  • Heparan Sulfate Proteoglycans / metabolism
  • Hexadimethrine Bromide / pharmacology
  • Humans
  • In Vitro Techniques
  • Molecular Sequence Data
  • Peptide Fragments / chemistry
  • Peptide Fragments / genetics
  • Polyelectrolytes
  • Polymers / pharmacology*
  • Virulence / drug effects
  • Virulence / genetics
  • Virus Replication

Substances

  • Anti-HIV Agents
  • CD4 Antigens
  • HIV Envelope Protein gp120
  • HIV envelope protein gp120 (305-321)
  • Heparan Sulfate Proteoglycans
  • Peptide Fragments
  • Polyelectrolytes
  • Polymers
  • polyanions
  • Hexadimethrine Bromide