HIV-1 and MLV Gag proteins are sufficient to recruit APOBEC3G into virus-like particles
HIV-1 and MLV Gag proteins are sufficient to recruit APOBEC3G into virus-like particles
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DOI：
10.1016/j.bbrc.2004.07.005
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发表时间：
2004-08-27
影响因子：
3.1
通讯作者：
Decroly, E
中科院分区：
文献类型：
--
作者：
Douaisi, M;Dussart, S;Decroly, E
胞苷脱氨酶hAPOBEC 3G是一种抗病毒人类因子，在不存在Vif蛋白的情况下抵消HIV-1的复制。hAPOBEC 3G被包装到病毒颗粒中并致死性地使HIV-1超突变。在这项工作中，我们研究的机制管理hAPOBEC 3G包装。通过GST pull-down和免疫共沉淀实验，我们发现hAPOBEC 3G与HIV-1 Pr 55 Gag及其NC结构域以及Pr 160 Gag-Pol中包含的RT和IN结构域结合。我们证明HIV-1 Gag的表达足以诱导hAPOBEC 3G包装成Gag颗粒。含有RT和IN结构域的Gag-Pol多肽以及HIV-1基因组RNA似乎不是hAPOBEC 3G包装所必需的。最后，我们表明，hAPOBEC 3G和它的小鼠直系同源物包装到HIV-1和MLV Gag颗粒。我们得出结论，Gag多肽从遥远的逆转录病毒具有保守的结构域，允许包装的主机抗病毒因子APOBEC 3G。(C)2004年爱思唯尔公司All rights reserved.
The cytidine deaminase hAPOBEC3G is an antiviral human factor that counteracts the replication of HIV-1 in absence of the Vif protein. hAPOBEC3G is packaged into virus particles and lethally hypermutates HIV-1. In this work, we examine the mechanisms governing hAPOBEC3G packaging. By GST pull-down and co-immunoprecipitation assays, we show that hAPOBEC3G binds to HIV-1 Pr55 Gag and its NC domain and to the RT and IN domains contained in Pr160 Gag-Pol. We demonstrate that the expression of HIV-1 Gag is sufficient to induce the packaging of hAPOBEC3G into Gag particles. Gag-Pol polypeptides containing RT and IN domains, as well as HIV-1 genomic RNA, seem not to be necessary for hAPOBEC3G packaging. Lastly, we show that hAPOBEC3G and its murine ortholog are packaged into HIV-1 and MLV Gag particles. We conclude that the Gag polypeptides from distant retroviruses have conserved domains allowing the packaging of the host antiviral factor APOBEC3G. (C) 2004 Elsevier Inc. All rights reserved.