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Published online October 16, 2003
Submitted on July 24, 2003 Induction of APOBEC3G Ubiquitination and Degradation by an HIV-1 Vif-Cul5-SCF Complex
1 Department of Molecular Microbiology and Immunology, Johns Hopkins University Bloomberg School of Public Health, Baltimore, MD 21205, USA; Jilin University, Jilin, P.R. China. * To whom correspondence should be addressed. E-mail: xfyu@jhsph.edu. HIV-1 Vif is essential for viral evasion of host antiviral factor CEM15/APOBEC3G. We now report that Vif interacts with cellular proteins Cul5, Elongins B and C, and Rbx1 to form an Skp1-Cullin-F-box (SCF)-like complex. The ability of Vif to suppress antiviral activity of APOBEC3G was specifically dependent on Cul5-SCF function, allowing Vif to interact with APOBEC3G and induce its ubiquitination and degradation. A Vif mutant that interacted with APOBEC3G but not with Cul5-SCF was functionally inactive. The Cul5-SCF was also required for Vif function in distantly related SIVmac/HIV-2. These results indicate that the conserved Cul5-SCF pathway used by Vif is a potential target for antiviral development.
Science 10.1126/science.1089591 Copyright © 2003 by The American Association for the Advancement of Science. All rights reserved. |
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