HIV-1 核壳蛋白在不同成熟状态下的核酸结合特性概述。
Overview of the Nucleic-Acid Binding Properties of the HIV-1 Nucleocapsid Protein in Its Different Maturation States.
机构信息
Expression Génétique Microbienne, UMR 8261, CNRS, Université de Paris, Institut de Biologie Physico-Chimique (IBPC), 75005 Paris, France.
Laboratoire de Biologie et de Pharmacologie Appliquée (LBPA), UMR 8113 CNRS, Institut D'Alembert, École Normale Supérieure Paris-Saclay, Université Paris-Saclay, 4, Avenue des Sciences, 91190 Gif sur Yvette, France.
出版信息
Viruses. 2020 Sep 29;12(10):1109. doi: 10.3390/v12101109.
HIV-1 Gag polyprotein orchestrates the assembly of viral particles. Its C-terminus consists of the nucleocapsid (NC) domain that interacts with nucleic acids, and p1 and p6, two unstructured regions, p6 containing the motifs to bind ALIX, the cellular ESCRT factor TSG101 and the viral protein Vpr. The processing of Gag by the viral protease subsequently liberates NCp15 (NC-p1-p6), NCp9 (NC-p1) and NCp7, NCp7 displaying the optimal chaperone activity of nucleic acids. This review focuses on the nucleic acid binding properties of the NC domain in the different maturation states during the HIV-1 viral cycle.
HIV-1 Gag 多聚蛋白协调病毒颗粒的组装。其 C 端由核衣壳（NC）结构域组成，该结构域与核酸相互作用，以及 p1 和 p6 两个非结构区域，p6 包含与 ALIX、细胞 ESCRT 因子 TSG101 和病毒蛋白 Vpr 结合的基序。病毒蛋白酶对 Gag 的加工随后释放 NCp15（NC-p1-p6）、NCp9（NC-p1）和 NCp7，NCp7 显示出核酸的最佳伴侣活性。本综述重点介绍 HIV-1 病毒周期中不同成熟状态下 NC 结构域的核酸结合特性。
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