Rev
Tat
Vif
Integrase
Proteomics
Env
Nef

Vif

The accessory protein Vif inactivates cellular cytidine deaminases A3F and A3G (members of the APOBEC3 family) that would otherwise cause extensive incorporation of deoxyuridines into the viral genome, leading to a high mutation rate and destroying key viral functions. Vif recruits A3G and A3F to a cellular ubiquitin protein ligase (E3 ligase) that includes Cullin-5, Ring-box 1 and Elongins B and C, ultimately leading to ubiquitination of A3G and A3F and their destruction by the proteosome. The HARC Center Vif project, headed by Dr. B. Matija Peterlin and Dr. John Gross, aims to elucidate the structural nature of Vif-mediated interactions that target APOBEC cytidine deaminases for destruction by the proteasome, as well as to better understand the antiviral activity of the APOBEC proteins themselves.