Implication for alphavirus host-cell entry and assembly indicated by a 3.5 angstrom resolution cryo-EM structure

文献类型： 外文期刊

第一作者： Chen, Lihong

作者： Chen, Lihong;Zhu, Dongjie;Ma, Jun;Kong, Lingfei;Zhang, Xinzheng;Chen, Lihong;Wang, Ming;Sun, Zhenzhao;Wang, Shida;Liu, Zaisi;Wei, Lili;Wang, Jingfei;Chen, Lihong;Zhang, Xinzheng;Zhu, Dongjie;Wang, Jinglin;He, Yuwen

作者机构：

期刊名称：NATURE COMMUNICATIONS （ 影响因子：14.919； 五年影响因子：15.805 ）

ISSN： 2041-1723

年卷期： 2018 年 9 卷

页码：

收录情况： SCI

摘要： Alphaviruses are enveloped RNA viruses that contain several human pathogens. Due to intrinsic heterogeneity of alphavirus particles, a high resolution structure of the virion is currently lacking. Here we provide a 3.5 angstrom cryo-EM structure of Sindbis virus, using block based reconstruction method that overcomes the heterogeneity problem. Our structural analysis identifies a number of conserved residues that play pivotal roles in the virus life cycle. We identify a hydrophobic pocket in the subdomain D of E2 protein that is stabilized by an unknown pocket factor near the viral membrane. Residues in the pocket are conserved in different alphaviruses. The pocket strengthens the interactions of the E1/E2 heterodimer and may facilitate virus assembly. Our study provides structural insights into alphaviruses that may inform the design of drugs and vaccines.

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