Title |
The dimerization domain of HIV-1 viral infectivity factor Vif is required to block virion incorporation of APOBEC3G
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Published in |
Retrovirology, November 2007
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DOI | 10.1186/1742-4690-4-81 |
Pubmed ID | |
Authors |
James H Miller, Vlad Presnyak, Harold C Smith |
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. |
Mendeley readers
Geographical breakdown
Country | Count | As % |
---|---|---|
United States | 3 | 5% |
Brazil | 3 | 5% |
France | 1 | 2% |
Spain | 1 | 2% |
Unknown | 51 | 86% |
Demographic breakdown
Readers by professional status | Count | As % |
---|---|---|
Student > Ph. D. Student | 15 | 25% |
Researcher | 14 | 24% |
Student > Bachelor | 7 | 12% |
Student > Master | 7 | 12% |
Student > Doctoral Student | 3 | 5% |
Other | 10 | 17% |
Unknown | 3 | 5% |
Readers by discipline | Count | As % |
---|---|---|
Agricultural and Biological Sciences | 31 | 53% |
Chemistry | 7 | 12% |
Biochemistry, Genetics and Molecular Biology | 7 | 12% |
Medicine and Dentistry | 3 | 5% |
Nursing and Health Professions | 1 | 2% |
Other | 6 | 10% |
Unknown | 4 | 7% |