AIP1/ALIX Is a Binding Partner for HIV-1 p6 and EIAV p9 Functioning in Virus Budding

Cell. 2003 Sep 19;114(6):689-99. doi: 10.1016/s0092-8674(03)00653-6.

Abstract

HIV-1 and other retroviruses exit infected cells by budding from the plasma membrane, a process requiring membrane fission. The primary late assembly (L) domain in the p6 region of HIV-1 Gag mediates the detachment of the virion by recruiting host Tsg101, a component of the class E vacuolar protein sorting (Vps) machinery. We now show that HIV Gag p6 contains a second region involved in L domain function that binds AIP1, a homolog of the yeast class E Vps protein Bro1. Further, AIP1 interacts with Tsg101 and homologs of a subunit of the yeast class E Vps protein complex ESCRT-III. AIP1 also binds to the L domain in EIAV p9, and this binding correlates perfectly with L domain function. These observations identify AIP1 as a component of the viral budding machinery, which serves to link a distinct region in the L domain of HIV-1 p6 and EIAV p9 to ESCRT-III.

Publication types

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

MeSH terms

  • Adenosine Triphosphatases / genetics
  • Adenosine Triphosphatases / metabolism
  • Binding Sites / genetics
  • Cell Membrane / metabolism
  • Cell Membrane / virology
  • DNA-Binding Proteins / genetics
  • DNA-Binding Proteins / metabolism
  • Endosomal Sorting Complexes Required for Transport
  • Gene Products, gag / genetics
  • Gene Products, gag / metabolism*
  • HIV-1 / genetics
  • HIV-1 / metabolism*
  • HeLa Cells
  • Humans
  • Infectious Anemia Virus, Equine / genetics
  • Infectious Anemia Virus, Equine / metabolism*
  • Microfilament Proteins / genetics
  • Microfilament Proteins / metabolism*
  • Microscopy, Electron
  • Nuclear Proteins / genetics
  • Nuclear Proteins / metabolism
  • Protein Binding / genetics
  • Protein Structure, Tertiary / genetics
  • Recombinant Fusion Proteins / genetics
  • Recombinant Fusion Proteins / metabolism
  • Saccharomyces cerevisiae Proteins / genetics
  • Saccharomyces cerevisiae Proteins / metabolism
  • Simian Immunodeficiency Virus / genetics
  • Simian Immunodeficiency Virus / metabolism
  • Transcription Factors / genetics
  • Transcription Factors / metabolism
  • Virus Shedding / physiology*
  • gag Gene Products, Human Immunodeficiency Virus

Substances

  • CHMP1A protein, human
  • DNA-Binding Proteins
  • Endosomal Sorting Complexes Required for Transport
  • Gene Products, gag
  • Microfilament Proteins
  • Nuclear Proteins
  • Recombinant Fusion Proteins
  • Saccharomyces cerevisiae Proteins
  • Transcription Factors
  • Tsg101 protein
  • VPS4 protein, S cerevisiae
  • actin interacting protein 1
  • gag Gene Products, Human Immunodeficiency Virus
  • p6 gag protein, Human immunodeficiency virus 1
  • Adenosine Triphosphatases