Crystal structure of the rabies virus nucleoprotein-RNA complex
Crystal structure of the rabies virus nucleoprotein-RNA complex
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DOI：
10.1126/science.1125280
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发表时间：
2006-07-21
期刊：
影响因子：
56.9
通讯作者：
Ruigrok, Rob W. H.
中科院分区：
文献类型：
--
作者：
Albertini, Aurelie A. V.;Wernimont, Amy K.;Ruigrok, Rob W. H.
负链RNA病毒将其基因组浓缩成螺旋核蛋白-RNA复合体--核衣壳，该复合体被包装成病毒粒子，并作为依赖RNA的RNA聚合酶复合体的模板。重组狂犬病病毒核蛋白-RNA复合体的晶体结构以3.5埃的分辨率被测定。核蛋白的聚合是通过原始体之间的结构域交换实现的，柔性铰链允许核衣壳的形成。核蛋白的两个核心域在它们的界面上夹住RNA，使其免受环境的影响。核蛋白对RNA的隔离可能是负链RNA病毒在感染周期的特定阶段保护其基因组免受针对病毒RNA的人类宿主细胞的先天免疫反应的一种常见机制。
Negative-strand RNA viruses condense their genome into a helical nucleoprotein-RNA complex, the nucleocapsid, which is packed into virions and serves as a template for the RNA-dependent RNA polymerase complex. The crystal structure of a recombinant rabies virus nucleoprotein-RNA complex, organized in an undecameric ring, has been determined at 3.5 angstrom resolution. Polymerization of the nucleoprotein is achieved by domain exchange between protomers, with flexible hinges allowing nucleocapsid formation. The two core domains of the nucleoprotein clamp around the RNA at their interface and shield it from the environment. RNA sequestering by nucleoproteins is likely a common mechanism used by negative-strand RNA viruses to protect their genomes from the innate immune response directed against viral RNA in human host cells at certain stages of an infectious cycle.