Histone chaperone CAF-1 promotes HIV-1 latency by leading the formation of phase-separated suppressive nuclear bodies

EMBO J. 2021 May 17;40(10):e106632. doi: 10.15252/embj.2020106632. Epub 2021 Mar 19.

Abstract

HIV-1 latency is a major obstacle to achieving a functional cure for AIDS. Reactivation of HIV-1-infected cells followed by their elimination via immune surveillance is one proposed strategy for eradicating the viral reservoir. However, current latency-reversing agents (LRAs) show high toxicity and low efficiency, and new targets are needed to develop more promising LRAs. Here, we found that the histone chaperone CAF-1 (chromatin assembly factor 1) is enriched on the HIV-1 long terminal repeat (LTR) and forms nuclear bodies with liquid-liquid phase separation (LLPS) properties. CAF-1 recruits epigenetic modifiers and histone chaperones to the nuclear bodies to establish and maintain HIV-1 latency in different latency models and primary CD4+ T cells. Three disordered regions of the CHAF1A subunit are important for phase-separated CAF-1 nuclear body formation and play a key role in maintaining HIV-1 latency. Disruption of phase-separated CAF-1 bodies could be a potential strategy to reactivate latent HIV-1.

Keywords: CAF-1; HIV-1 latency; epigenetic regulation; nuclear body; phase separation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • CD4-Positive T-Lymphocytes / metabolism
  • Chromatin Assembly Factor-1 / genetics
  • Chromatin Assembly Factor-1 / metabolism
  • Epigenesis, Genetic / genetics
  • Epigenesis, Genetic / physiology
  • HEK293 Cells
  • HIV-1 / metabolism*
  • Humans
  • Promoter Regions, Genetic / genetics

Substances

  • CHAF1A protein, human
  • Chromatin Assembly Factor-1

Associated data

  • GEO/GSE166337