Induction of APOBEC3G Ubiquitination and Degradation by an HIV-1 Vif-Cul5-SCF Complex

Author:

Yu Xianghui123,Yu Yunkai123,Liu Bindong123,Luo Kun123,Kong Wei123,Mao Panyong123,Yu Xiao-Fang123

Affiliation:

1. Department of Molecular Microbiology and Immunology, Bloomberg School of Public Health, Johns Hopkins University, Baltimore, MD 21205, USA.

2. Jilin University, Jilin, People's Republic of China.

3. Zhejiang University, Zhejiang, People's Republic of China.

Abstract

Human immunodeficiency virus–1 (HIV-1) Vif is essential for viral evasion of host antiviral factor CEM15/APOBEC3G. We 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 simian immunodeficiency virus mac. These results indicate that the conserved Cul5-SCF pathway used by Vif is a potential target for antiviral development.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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