Journal
VIROLOGY
Volume 328, Issue 2, Pages 163-168Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.virol.2004.08.006
Keywords
HIV-1; APOBEC3G; virion incorporation; RNA binding
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Funding
- NIAID NIH HHS [AI057099] Funding Source: Medline
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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. (C) 2004 Elsevier Inc. All rights reserved.
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