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Induction of APOBEC3G ubiquitination and degradation by an HIV-1 Vif-Cul5-SCF complex
- Source :
- Science (New York, N.Y.). 302(5647)
- Publication Year :
- 2003
-
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.
- Subjects :
- Cytidine deaminase activity
Gene Products, vif
viruses
Elongin
APOBEC-3G Deaminase
Nucleoside Deaminases
Biology
Transfection
Virus Replication
Cell Line
SCF complex
Cytidine deamination
Cytidine Deaminase
vif Gene Products, Human Immunodeficiency Virus
Animals
Humans
APOBEC3A
APOBEC3G
Multidisciplinary
Ubiquitin
virus diseases
Proteins
biochemical phenomena, metabolism, and nutrition
Cullin Proteins
Virology
Viral infectivity factor
Repressor Proteins
embryonic structures
Mutation
HIV-1
Carrier Proteins
CUL5
Transcription Factors
Subjects
Details
- ISSN :
- 10959203
- Volume :
- 302
- Issue :
- 5647
- Database :
- OpenAIRE
- Journal :
- Science (New York, N.Y.)
- Accession number :
- edsair.doi.dedup.....62f4daf25b87ee038b56b2e64708bd5e