Mechanism of resistance to and regulation of APOBEC3 antiviral activity

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In the field of viral-host interactions, the interplay of the antiviral cytidine-deaminating enzyme APOBEC3 and retroviruses is a rather new area of research. The human immunodeficiency virus (HIV), a lentivirus, counteracts the anti-viral activity of APOBEC-3F/-3G by its protein Vif. Vif induces a proteasomal degradation of APOBEC3. Recently we discovered that foamy viruses, which belong to another retrovirus subfamily, also neutralize APOBEC3 proteins by an accessory protein, called Bet. Preliminary data indicate that APOBEC3 suppression by Bet does not involve protein degradation. The first aim is to analyse the mechanism of how Bet protects retroviruses against APOBEC3. Unknown as well is the post-translational regulation of APOBEC3G activity. In the second project we will investigate the role of host-cell regulated phosphorylation of Vif, Bet and APOBEC3 for its functions. A better understanding of the interactions of Vif-APOBEC3 and Bet-APOBEC3 may pose an avenue for future anti HIV-1 drug discovery and development.