对病毒感染因子（Vif）蛋白结构认识的进展。
Advances in the structural understanding of Vif proteins.
作者信息
Barraud Pierre, Paillart Jean-Christophe, Marquet Roland, Tisné Carine
机构信息
Laboratoire de Cristallographie et RMN biologiques, Université Paris-Descartes, CNRS UMR 8015, Paris, France.
出版信息
Curr HIV Res. 2008 Mar;6(2):91-9. doi: 10.2174/157016208783885056.
Abstract
The multidomain HIV-1 Vif protein recruits several cellular partners to achieve neutralization of the antiviral activity of APOBEC3 proteins. Vif neutralizes APOBEC3G and APOBEC3F predominantly by forming an E3 ubiquitin ligase with Cullin5, ElonginB and ElonginC that targets these proteins for degradation by the ubiquitin-proteasome pathway. Vif associates with the Cullin5-ElonginB-ElonginC complex by binding directly to ElonginC via its SOCS-box motif and to Cullin5 via hydrophobic residues within a zinc-binding region formed by a conserved HCCH motif. The HIV-1 Vif-Cullin5-ElonginBC complex is then able to ubiquitinate the APOBEC3G factor bound to Vif by its N-terminal domain. In this review, we summarize the current knowledge about the structural determinants of Vif that allow it to interact with cellular and viral partners.
摘要
多结构域的HIV-1 Vif蛋白招募多个细胞伴侣以中和APOBEC3蛋白的抗病毒活性。Vif主要通过与Cullin5、ElonginB和ElonginC形成E3泛素连接酶，将这些蛋白靶向通过泛素-蛋白酶体途径降解，从而中和APOBEC3G和APOBEC3F。Vif通过其SOCS盒基序直接与ElonginC结合，并通过由保守的HCCH基序形成的锌结合区域内的疏水残基与Cullin5结合，从而与Cullin5-ElonginB-ElonginC复合物结合。然后，HIV-1 Vif-Cullin5-ElonginBC复合物能够通过其N端结构域将与Vif结合的APOBEC3G因子泛素化。在本综述中，我们总结了目前关于Vif结构决定因素的知识，这些因素使其能够与细胞和病毒伴侣相互作用。
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