Structure of Ljungan virus provides insight into genome packaging of this picornavirus.
Structure of Ljungan virus provides insight into genome packaging of this picornavirus.
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Ljungan 病毒的结构提供了对该小核糖核酸病毒基因组包装的深入了解
DOI：
10.1038/ncomms9316
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发表时间：
2015-10-08
影响因子：
16.6
通讯作者：
Stuart DI
中科院分区：
文献类型：
--
作者：
Zhu L;Wang X;Ren J;Porta C;Wenham H;Ekström JO;Panjwani A;Knowles NJ;Kotecha A;Siebert CA;Lindberg AM;Fry EE;Rao Z;Tuthill TJ;Stuart DI
小核糖核酸病毒是一系列人类和动物疾病的罪魁祸首，但其RNA基因组如何包装仍然知之甚少。在这个家族中，一个特别缺乏研究的群体是那些缺乏内部外壳蛋白VP 4的人。在这里，我们报告了一种这样的病毒，Ljungan病毒，ParechovirusB属的类型成员的原子结构，它与人类的糖尿病和心肌炎有关。3.78-kDa分辨率的冷冻电子显微镜结构显示出显著的特征，包括延伸的VP 1 C末端，在病毒的外表面上形成主要突起，以及在VP 3的N末端的基本基序，结合到约12%的病毒基因组。这种明显的电荷驱动的RNA附着表明，小核糖核酸病毒的这个分支使用不同的基因组折叠机制，这可能是在小核糖核酸病毒进化的早期探索的。
Picornaviruses are responsible for a range of human and animal diseases, but how their RNA genome is packaged remains poorly understood. A particularly poorly studied group within this family are those that lack the internal coat protein, VP4. Here we report the atomic structure of one such virus, Ljungan virus, the type member of the genusParechovirusB, which has been linked to diabetes and myocarditis in humans. The 3.78-Å resolution cryo-electron microscopy structure shows remarkable features, including an extended VP1 C terminus, forming a major protuberance on the outer surface of the virus, and a basic motif at the N terminus of VP3, binding to which orders some 12% of the viral genome. This apparently charge-driven RNA attachment suggests that this branch of the picornaviruses uses a different mechanism of genome encapsidation, perhaps explored early in the evolution of picornaviruses.