Abstract |
In cells infected by HIV-1 mutants lacking a functional Vif protein, APOBEC3G is specifically packaged into progeny virions and then interferes with the process of virus infection. Here, we show that incorporation of APOBEC3G into HIV-1 virions is mediated by the specific interaction of APOBEC3G with the carboxy-terminal nucleocapsid/p6 domain of the Gag polyprotein precursor. As a result, HIV-1 virus-like particles that lack the nucleocapsid domain fail to package APOBEC3G. Surprisingly, RNA was also found to be essential for formation of the nucleocapsid--APOBEC3G complex in vitro, thus raising the possibility that RNA may form a bridge between these two proteins.
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Authors | Alexandra Schäfer, Hal P Bogerd, Bryan R Cullen |
Journal | Virology
(Virology)
Vol. 328
Issue 2
Pg. 163-8
(Oct 25 2004)
ISSN: 0042-6822 [Print] United States |
PMID | 15464836
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, P.H.S.)
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Chemical References |
- Gene Products, gag
- Gene Products, vif
- Protein Precursors
- Proteins
- RNA, Viral
- Repressor Proteins
- vif Gene Products, Human Immunodeficiency Virus
- Nucleoside Deaminases
- APOBEC-3G Deaminase
- APOBEC3G protein, human
- Cytidine Deaminase
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Topics |
- APOBEC-3G Deaminase
- Cell Line, Transformed
- Cytidine Deaminase
- Gene Products, gag
(metabolism)
- Gene Products, vif
(genetics)
- HIV-1
(genetics, physiology)
- Nucleocapsid
(metabolism)
- Nucleoside Deaminases
- Protein Precursors
(metabolism)
- Protein Structure, Tertiary
- Proteins
(metabolism)
- RNA, Viral
(metabolism)
- Repressor Proteins
- Virion
(physiology)
- Virus Assembly
- vif Gene Products, Human Immunodeficiency Virus
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