Dual Functionality of HIV-1 Vif in APOBEC3 Counteraction and Cell Cycle Arrest

Daniel J. Salamango, Reuben S. Harris

Research output: Contribution to journalReview articlepeer-review

14 Scopus citations


Accessory proteins are a key feature that distinguishes primate immunodeficiency viruses such as human immunodeficiency virus type I (HIV-1) from other retroviruses. A prime example is the virion infectivity factor, Vif, which hijacks a cellular co-transcription factor (CBF-β) to recruit a ubiquitin ligase complex (CRL5) to bind and degrade antiviral APOBEC3 enzymes including APOBEC3D (A3D), APOBEC3F (A3F), APOBEC3G (A3G), and APOBEC3H (A3H). Although APOBEC3 antagonism is essential for viral pathogenesis, and a more than sufficient functional justification for Vif’s evolution, most viral proteins have evolved multiple functions. Indeed, Vif has long been known to trigger cell cycle arrest and recent studies have shed light on the underlying molecular mechanism. Vif accomplishes this function using the same CBF-β/CRL5 ubiquitin ligase complex to degrade a family of PPP2R5 phospho-regulatory proteins. These advances have helped usher in a new era of accessory protein research and fresh opportunities for drug development.

Original languageEnglish (US)
Article number622012
JournalFrontiers in Microbiology
StatePublished - Jan 12 2021
Externally publishedYes


  • PPP2R5
  • Vif
  • cell cycle arrest

ASJC Scopus subject areas

  • Microbiology (medical)
  • Microbiology


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