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现在位置:首页 > 科研进展 > 最新重要论文(影响因子PNAS及以上)
Implication for alphavirus host-cell entry and assembly indicated by a 3.5? resolution cryo-EM structure, Nat Commun, 14 Dec 2018
2018-12-14 | 【     】【打印】【关闭

Nature Communications, 14 December 2018

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

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

Abstract

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? 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.

文章链接:https://www.nature.com/articles/s41467-018-07704-x

相关报道:http://www.ibp.cas.cn/kyjz/zxdt/201812/t20181213_5211882.html

 

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