Structural Insights into Alphavirus Assembly Revealed by the Cryo-EM Structure of Getah Virus

文献类型： 外文期刊

第一作者： Wang, Ming

作者： Wang, Ming;Sun, Zhenzhao;Wang, Shida;Yang, Decheng;Shi, Zhibin;Wei, Xinyu;Wang, Pengfei;Sun, Weiyao;Zhu, Jing;Li, Jiaqi;Du, Bingchen;Liu, Zaisi;Wei, Lili;Liu, Chunguo;He, Xijun;Wang, Jingfei;Cui, Chenxi;Wang, Xiangxi;Zhang, Xinzheng

作者机构：

关键词： alphavirus; Getah virus; cryo-EM; viral assembly; block-based reconstruction

期刊名称：VIRUSES-BASEL （ 影响因子：5.818； 五年影响因子：5.811 ）

ISSN：

年卷期： 2022 年 14 卷 2 期

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收录情况： SCI

摘要： Getah virus (GETV) is a member of the alphavirus genus, and it infects a variety of animal species, including horses, pigs, cattle, and foxes. Human infection with this virus has also been reported. The structure of GETV has not yet been determined. In this study, we report the cryo-EM structure of GETV at a resolution of 3.5 angstrom. This structure reveals conformational polymorphism of the envelope glycoproteins E1 and E2 at icosahedral 3-fold and quasi-3-fold axes, which is believed to be a necessary organization in forming a curvature surface of virions. In our density map, three extra densities are identified, one of which is believed a "pocket factor"; the other two are located by domain D of E2, and they may maintain the stability of E1/E2 heterodimers. We also identify three N-glycosylations at E1 N141, E2 N200, and E2 N262, which might be associated with receptor binding and membrane fusion. The resolving of the structure of GETV provides new insights into the structure and assembly of alphaviruses and lays a basis for studying the differences of biology and pathogenicity between arthritogenic and encephalitic alphaviruses.

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