HIV latency is reversed by ACSS2-driven histone crotonylation

J Clin Invest. 2018 Mar 1;128(3):1190-1198. doi: 10.1172/JCI98071. Epub 2018 Feb 19.

Abstract

Eradication of HIV-1 (HIV) is hindered by stable viral reservoirs. Viral latency is epigenetically regulated. While the effects of histone acetylation and methylation at the HIV long-terminal repeat (LTR) have been described, our knowledge of the proviral epigenetic landscape is incomplete. We report that a previously unrecognized epigenetic modification of the HIV LTR, histone crotonylation, is a regulator of HIV latency. Reactivation of latent HIV was achieved following the induction of histone crotonylation through increased expression of the crotonyl-CoA-producing enzyme acyl-CoA synthetase short-chain family member 2 (ACSS2). This reprogrammed the local chromatin at the HIV LTR through increased histone acetylation and reduced histone methylation. Pharmacologic inhibition or siRNA knockdown of ACSS2 diminished histone crotonylation-induced HIV replication and reactivation. ACSS2 induction was highly synergistic in combination with either a protein kinase C agonist (PEP005) or a histone deacetylase inhibitor (vorinostat) in reactivating latent HIV. In the SIV-infected nonhuman primate model of AIDS, the expression of ACSS2 was significantly induced in intestinal mucosa in vivo, which correlated with altered fatty acid metabolism. Our study links the HIV/SIV infection-induced fatty acid enzyme ACSS2 to HIV latency and identifies histone lysine crotonylation as a novel epigenetic regulator for HIV transcription that can be targeted for HIV eradication.

Keywords: AIDS/HIV; Infectious disease; Transcription.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetate-CoA Ligase / genetics*
  • Animals
  • CD4-Positive T-Lymphocytes / cytology
  • CD4-Positive T-Lymphocytes / virology
  • Chromatin / chemistry
  • Epigenesis, Genetic
  • Fatty Acids / metabolism
  • HIV Infections / drug therapy*
  • HIV-1 / physiology
  • Histones / metabolism*
  • Humans
  • Jurkat Cells
  • Leukocytes, Mononuclear / virology
  • RNA, Small Interfering / metabolism
  • Signal Transduction
  • Simian Immunodeficiency Virus / drug effects
  • Terminal Repeat Sequences
  • Virus Latency / drug effects*
  • Vorinostat / pharmacology

Substances

  • Chromatin
  • Fatty Acids
  • Histones
  • RNA, Small Interfering
  • Vorinostat
  • ACSS2 protein, human
  • Acetate-CoA Ligase