Human immunodeficiency virus type 1 virion infectivity factor (HIV-1 Vif) (HIV-1 Vif)

Human immunodeficiency virus type 1 (HIV-1) Virion infectivity factor (Vif) is a 23-kDa accessory protein essential for viral pathogenesis (UniProt: P12504). Its primary biological function is to counteract the host's innate antiviral defense mediated by the APOBEC3 family of cytidine deaminases, particularly APOBEC3G (PubMed: 12855938). Vif acts as an adaptor that recruits a Cullin5-based E3 ubiquitin ligase complex to target APOBEC3G for polyubiquitination and subsequent proteasomal degradation (PubMed: 14702096). By preventing the incorporation of APOBEC3G into budding virions, Vif ensures the production of infectious progeny. In the absence of Vif, APOBEC3G induces extensive G-to-A hypermutations in the viral cDNA during reverse transcription, leading to non-functional viral genomes (PubMed: 15247912). Consequently, the conserved regions of Vif, such as the HCCH and SLQ motifs, are attractive targets for antiretroviral therapy (PubMed: 22101657). Small molecule inhibitors designed to disrupt the Vif-APOBEC3G interaction or the Vif-CBFβ assembly aim to restore the host's natural immunity against HIV-1 (PubMed: 25406361).

Other names

VifVirion infectivity factorp23HIV-1 Vif proteinVif conserved region

Inhibition of Vif-mediated degradation of APOBEC3G by disrupting Vif's interaction with APOBEC3G or its E3 ubiquitin ligase co-factors (e.g., CBFβ, Cullin5), thereby restoring host innate immunity.