Identification of the glycoprotein 41(TM) cytoplasmic tail domains of human immunodeficiency virus type 1 that interact with Pr55Gag particles

AIDS Res Hum Retroviruses. 2000 Aug 10;16(12):1141-7. doi: 10.1089/088922200414983.

Abstract

We investigated the protein/protein interactions that occur during human immunodeficiency virus (HIV-1) budding. We evaluated the binding to Pr55Gag particles of peptides mapping to the cytoplasmic tail of gp41TM and of host-cell proteins, in a cell-free, in vitro assay. Host-cell proteins and irrelevant viral envelope peptides did not bind. Peptides corresponding to a large central domain of the gp41TM cytoplasmic tail (93 residues) bound to Pr55Gag particles. This demonstrates that a Gag/Env interaction is responsible for the specific incorporation of the Env glycoprotein into nascent HIV-1 virions, and defines more accurately the gp41TM domain involved in this interaction.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Cell Line
  • Cell Membrane / ultrastructure
  • Cell Membrane / virology
  • Cricetinae
  • Gene Products, gag / chemistry*
  • Gene Products, gag / metabolism*
  • HIV Envelope Protein gp41 / chemistry*
  • HIV Envelope Protein gp41 / metabolism*
  • HIV-1 / growth & development
  • HIV-1 / physiology*
  • HIV-1 / ultrastructure
  • Humans
  • Molecular Sequence Data
  • Peptide Fragments / chemistry
  • Peptide Fragments / metabolism
  • Peptide Mapping
  • Protein Precursors / chemistry*
  • Protein Precursors / metabolism*
  • Transfection

Substances

  • Gene Products, gag
  • HIV Envelope Protein gp41
  • Peptide Fragments
  • Protein Precursors
  • p55 gag precursor protein, Human immunodeficiency virus 1