Host cyclophilin A mediates HIV-1 attachment to target cells via heparans

EMBO J. 1999 Dec 1;18(23):6771-85. doi: 10.1093/emboj/18.23.6771.

Abstract

The present study proposes a novel mode of action for cyclophilin A (CypA) in the HIV-1 life cycle. We demonstrate that CypA-deficient viruses do not replicate because they fail to attach to target cells. We show that CypA is exposed at the viral membrane and mediates HIV-1 attachment. We identify heparan as the exclusive cellular binding partner for CypA. Furthermore, CypA binds directly to heparan via a domain rich in basic residues similar to known heparin-binding motifs. This interaction between exposed CypA and cell surface heparans represents the initial step of HIV-1 attachment and is a necessary precursor to gp120-binding to CD4. In conclusion, HIV-1 attachment to target cells is a multi-step process that requires an initial CypA-heparan interaction followed by the gp120-CD4 interaction.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • CD4 Antigens / metabolism
  • CD4-Positive T-Lymphocytes / virology
  • Cell Line
  • Cell Membrane / metabolism
  • Glycosaminoglycans / metabolism*
  • HIV Envelope Protein gp120 / physiology*
  • HIV-1 / physiology*
  • HeLa Cells
  • Heparin / metabolism
  • Humans
  • Membrane Fusion
  • Peptidylprolyl Isomerase / metabolism*
  • Protein Binding
  • Subtilisin / metabolism
  • Transfection
  • Virion / physiology
  • Virus Assembly*
  • Virus Replication

Substances

  • CD4 Antigens
  • Glycosaminoglycans
  • HIV Envelope Protein gp120
  • Heparin
  • Subtilisin
  • Peptidylprolyl Isomerase