Antagonism of PP2A is an independent and conserved function of HIV-1 Vif and causes cell cycle arrest

Elife. 2020 Apr 15:9:e53036. doi: 10.7554/eLife.53036.

Abstract

The seminal description of the cellular restriction factor APOBEC3G and its antagonism by HIV-1 Vif has underpinned two decades of research on the host-virus interaction. We recently reported that HIV-1 Vif is also able to degrade the PPP2R5 family of regulatory subunits of key cellular phosphatase PP2A (PPP2R5A-E; Greenwood et al., 2016; Naamati et al., 2019). We now identify amino acid polymorphisms at positions 31 and 128 of HIV-1 Vif which selectively regulate the degradation of PPP2R5 family proteins. These residues covary across HIV-1 viruses in vivo, favouring depletion of PPP2R5A-E. Through analysis of point mutants and naturally occurring Vif variants, we further show that degradation of PPP2R5 family subunits is both necessary and sufficient for Vif-dependent G2/M cell cycle arrest. Antagonism of PP2A by HIV-1 Vif is therefore independent of APOBEC3 family proteins, and regulates cell cycle progression in HIV-infected cells.

Keywords: HIV; PP2A; Vif; cell cycle; infectious disease; microbiology; virus.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • APOBEC Deaminases / metabolism
  • Cell Cycle Checkpoints*
  • Flow Cytometry
  • HIV-1 / genetics*
  • HIV-1 / physiology
  • Host Microbial Interactions
  • Humans
  • Point Mutation / genetics
  • Protein Phosphatase 2 / metabolism*
  • vif Gene Products, Human Immunodeficiency Virus / genetics
  • vif Gene Products, Human Immunodeficiency Virus / physiology*

Substances

  • PPP2R5A protein, human
  • vif Gene Products, Human Immunodeficiency Virus
  • vif protein, Human immunodeficiency virus 1
  • Protein Phosphatase 2
  • APOBEC Deaminases
  • APOBEC3 proteins, human