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首页> 外文期刊>Journal of Molecular Biology >Interaction with 7SL RNA but not with HIV-1 genomic RNA or p bodies is required for APOBEC3F virion packaging
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Interaction with 7SL RNA but not with HIV-1 genomic RNA or p bodies is required for APOBEC3F virion packaging

机译:APOBEC3F病毒体包装要求与7SL RNA相互作用,但与HIV-1基因组RNA或p体不需要相互作用

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摘要

Human cytidine deaminase apolipoprotein B mRNA-editing catalytic polypeptide-like 3F (APOBEC3F, or A3F), like APOBEC3G, has broad antiviral activity against diverse retroelements, including Vif-deficient human immunodeficiency virus (HIV)-1. Its antiviral functions are known to rely on its virion encapsidation and be suppressed by HIV-1 Vif, which recruits Cullin5-based E3 ubiquitin ligases. However, the factors that mediate A3F virion packaging have not yet been identified. In this study, we demonstrate that A3F specifically interacts with cellular signal recognition particle (SRP) RNA (7SL RNA), which is selectively packaged into HIV-1 virions. Efficient packaging of 7SL RNA as well as A3F was mediated by the RNA-binding nucleocapsid domain of HIV-1 Gag. Reducing 7SL RNA packaging by overexpression of SRP19 protein inhibited A3F virion packaging. Although A3F has been shown to interact with P bodies and viral genomic RNA, our data indicated that P bodies and HIV-1 genomic RNA were not required for A3F packaging. Thus, in addition to its well-known function in SRPs, 7SL RNA, which is encapsidated into diverse retroviruses, also participates in the innate antiviral function of host cytidine deaminases. (c) 2007 Elsevier Ltd. All rights reserved.
机译:人胞苷脱氨酶载脂蛋白B mRNA编辑催化多肽样3F(APOBEC3F或A3F),如APOBEC3G,对包括Vif缺陷型人免疫缺陷病毒(HIV)-1在内的各种后代元素具有广泛的抗病毒活性。已知其抗病毒功能依赖于其病毒体衣壳,并被HIV-1 Vif抑制,后者募集了基于Cullin5的E3泛素连接酶。但是,尚未确定介导A3F病毒体包装的因素。在这项研究中,我们证明A3F与细胞信号识别颗粒(SRP)RNA(7SL RNA)特异性相互作用,后者被选择性地包装到HIV-1病毒粒子中。 HIV-1 Gag的RNA结合核衣壳结构域介导了7SL RNA和A3F的有效包装。通过过度表达SRP19蛋白减少7SL RNA包装可抑制A3F病毒体包装。尽管已显示A3F与P体和病毒基因组RNA相互作用,但我们的数据表明A3F包装不需要P体和HIV-1基因组RNA。因此,除了在SRP中众所周知的功能外,衣壳化为多种逆转录病毒的7SL RNA还参与了宿主胞嘧啶脱氨酶的先天抗病毒功能。 (c)2007 Elsevier Ltd.保留所有权利。

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