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HIV-1 matrix domain removal ameliorates virus assembly and processing defects incurred by positive nucleocapsid charge elimination

机译:HIV-1基质结构域的去除改善了核衣壳正电荷消除所引起的病毒装配和加工缺陷

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Human immunodeficiency virus type 1 nucleocapsid (NC) basic residues presumably contribute to virus assembly via RNA, which serves as a scaffold for Gag-Gag interaction during particle assembly. To determine whether NC basic residues play a role in Gag cleavage (thereby impacting virus assembly), Gag processing efficiency and virus particle production were analyzed for an HIV-1 mutant NC15A, with alanine serving as a substitute for all NC basic residues. Results indicate that NC15A significantly impaired virus maturation in addition to significantly affecting Gag membrane binding and assembly. Interestingly, removal of the matrix (MA) central globular domain ameliorated the NC15A assembly and processing defects, likely through enhancement of Gag multimerization and membrane binding capacities.
机译:人类免疫缺陷病毒1型核衣壳(NC)基本残基可能通过RNA参与了病毒组装,RNA在颗粒组装过程中充当了Gag-Gag相互作用的支架。为了确定NC基本残基是否在Gag裂解中起作用(从而影响病毒装配),分析了HIV-1突变型NC15A的Gag加工效率和病毒颗粒产生,其中丙氨酸替代了所有NC基本残基。结果表明,NC15A除了显着影响Gag膜的结合和组装外,还大大损害了病毒的成熟度。有趣的是,去除基质(MA)中心球状结构域可以改善NC15A组装和加工缺陷,这可能是通过增强Gag多聚化和膜结合能力来实现的。

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