Heat-shock proteins reverse the G2 arrest caused by HIV-1 viral protein R.
HIV-1 Vpr is an important contributor to viral pathogenesis. Vpr displays several highly conserved pathogenic activities, including induction of cell cycle G(2) arrest and cell death. The host immune system, in turn, preferentially targets Vpr in an attempt to reduce its pathogenic effects. To identify innate anti-Vpr factors, we performed a genetic search for multicopy suppressors of Vpr-induced G(2) arrest in fission yeast. Several heat-shock proteins were identified in these experiments. Analyses in mammalian cells demonstrated that heatshock proteins HSP27 and HSP70 suppress Vpr-induced G2 arrest. This effect appears to be mediated by an interaction between heat shock proteins and Vpr. These results illustrate another example of antagonistic interactions between the viral and cellular proteins.
Bukrinsky
Michael
M
Department of Microbiology and Tropical Medicine, The George Washington University, Washington, DC 20037, USA. mtmmib@gwumc.edu
Zhao
Yuqi
Y
D002478:Cells, Cultured; D016193:G1 Phase / Q000502:physiology; D016195:G2 Phase / Q000502:physiology*; D016336:Gene Products, vpr / Q000378:metabolism / Q000502:physiology*; D015497:HIV-1; D018840:HSP70 Heat-Shock Proteins / Q000378:metabolism / Q000502:physiology*; D006360:Heat-Shock Proteins / Q000378:metabolism / Q000502:physiology*; D006801:Humans; D012568:Schizosaccharomyces; D054325:vpr Gene Products, Human Immunodeficiency Virus
D016336:Gene Products, vpr; D018840:HSP70 Heat-Shock Proteins; D006360:Heat-Shock Proteins; D054325:vpr Gene Products, Human Immunodeficiency Virus