Implication for alphavirus host-cell entry and assembly indicated by a 3.5Å 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 () and Xinzheng Zhang ()
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Lihong Chen: Chinese Academy of Sciences
Ming Wang: Chinese Academy of Agricultural Sciences
Dongjie Zhu: Chinese Academy of Sciences
Zhenzhao Sun: Chinese Academy of Agricultural Sciences
Jun Ma: Chinese Academy of Sciences
Jinglin Wang: Yunnan Animal Science and Veterinary Institute
Lingfei Kong: Chinese Academy of Sciences
Shida Wang: Chinese Academy of Agricultural Sciences
Zaisi Liu: Chinese Academy of Agricultural Sciences
Lili Wei: Chinese Academy of Agricultural Sciences
Yuwen He: Yunnan Animal Science and Veterinary Institute
Jingfei Wang: Chinese Academy of Agricultural Sciences
Xinzheng Zhang: Chinese Academy of Sciences

Nature Communications, 2018, vol. 9, issue 1, 1-8

Abstract: 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 Å 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.

Date: 2018
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DOI: 10.1038/s41467-018-07704-x

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