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Advances in Virology
Volume 2010, Article ID 649315, 10 pages
Review Article

Towards Inhibition of Vif-APOBEC3G Interaction: Which Protein to Target?

URIA-Centro Patogénese Molecular and Instituto de Medicina Molecular, Faculdade de Farmácia da Universidade Lisboa, Avenue Das Forcas Armadas, 1649-019 Lisboa, Portugal

Received 2 May 2010; Revised 31 July 2010; Accepted 14 August 2010

Academic Editor: Michael Bukrinsky

Copyright © 2010 Iris Cadima-Couto and Joao Goncalves. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


APOBEC proteins appeared in the cellular battle against HIV-1 as part of intrinsic cellular immunity. The antiretroviral activity of some of these proteins is overtaken by the action of HIV-1 Viral Infectivity Factor (Vif) protein. Since the discovery of APOBEC3G (A3G) as an antiviral factor, many advances have been made to understand its mechanism of action in the cell and how Vif acts in order to counteract its activity. The mainstream concept is that Vif overcomes the innate antiviral activity of A3G by direct protein binding and promoting its degradation via the cellular ubiquitin/proteasomal pathway. Vif may also inhibit A3G through mechanisms independent of proteasomal degradation. Binding of Vif to A3G is essential for its degradation since disruption of this interaction is predicted to stimulate intracellular antiviral immunity. In this paper we will discuss the different binding partners between both proteins as one of the major challenges for the development of new antiviral drugs.