Specific packaging of APOBEC3G into HIV-1 virions is mediated by the nucleocapsid domain of the gag polyprotein precursor

被引:197
作者
Schäfer, A
Bogerd, HP
Cullen, BR
机构
[1] Duke Univ, Med Ctr, Howard Hughes Med Inst, Durham, NC 27710 USA
[2] Duke Univ, Med Ctr, Dept Mol Genet & Microbiol, Durham, NC 27710 USA
关键词
HIV-1; APOBEC3G; virion incorporation; RNA binding;
D O I
10.1016/j.virol.2004.08.006
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
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.
引用
收藏
页码:163 / 168
页数:6
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