Schäfer Alexandra, Bogerd Hal P, Cullen Bryan R
Howard Hughes Medical Institute and Department of Molecular Genetics and Microbiology, Duke University Medical Center, Durham, NC 27710, USA.
Virology. 2004 Oct 25;328(2):163-8. doi: 10.1016/j.virol.2004.08.006.
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.
在被缺乏功能性Vif蛋白的HIV-1突变体感染的细胞中，载脂蛋白B mRNA编辑酶催化多肽样蛋白3G（APOBEC3G）被特异性包装进子代病毒体，进而干扰病毒感染过程。在此，我们表明APOBEC3G掺入HIV-1病毒体是由APOBEC3G与Gag多蛋白前体的羧基末端核衣壳/p6结构域的特异性相互作用介导的。因此，缺乏核衣壳结构域的HIV-1病毒样颗粒无法包装APOBEC3G。令人惊讶的是，在体外还发现RNA对于核衣壳-APOBEC3G复合物的形成至关重要，从而增加了RNA可能在这两种蛋白质之间形成桥梁的可能性。
