We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
The dimerization domain of HIV-1 viral infectivity factor Vif is required to block virion incorporation of APOBEC3G.
- Authors
Miller, James H; Presnyak, Vlad; Smith, Harold C
- Abstract
The HIV-1 accessory protein known as viral infectivity factor or Vif binds to the host defence factor human APOBEC3G (hA3G) and prevents its assembly with viral particles and mediates its elimination through ubiquitination and degradation by the proteosomal pathway. In the absence of Vif, hA3G becomes incorporated within viral particles. During the post entry phase of infection, hA3G attenuates viral replication by binding to the viral RNA genome and deaminating deoxycytidines to form deoxyuridines within single stranded DNA regions of the replicated viral genome. Vif dimerization has been reported to be essential for viral infectivity but the mechanistic requirement for Vif multimerization is unknown.
- Publication
Retrovirology, 2007, Vol 4, p81
- ISSN
1742-4690
- Publication type
Journal Article
- DOI
10.1186/1742-4690-4-81