Induction of APOBEC3G ubiquitination and degradation by an HIV-1 Vif-Cul5-SCF complex.
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.
Mesh Terms:
Animals, Carrier Proteins, Cell Line, Cullin Proteins, Cytidine Deaminase, Gene Products, vif, HIV-1, Humans, Mutation, Nucleoside Deaminases, Proteins, Repressor Proteins, Transcription Factors, Transfection, Ubiquitin, Virus Replication, vif Gene Products, Human Immunodeficiency Virus
Animals, Carrier Proteins, Cell Line, Cullin Proteins, Cytidine Deaminase, Gene Products, vif, HIV-1, Humans, Mutation, Nucleoside Deaminases, Proteins, Repressor Proteins, Transcription Factors, Transfection, Ubiquitin, Virus Replication, vif Gene Products, Human Immunodeficiency Virus
Science
Date: Nov. 07, 2003
PubMed ID: 14564014
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