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Implication for alphavirus host-cell entry and assembly indicated by a 3.5Å resolution cryo-EM structure. Nat Commun. 2018 Dec14;9(1):5326

Chen  , Wang M , Zhu D , Sun Z , Ma J , Wang J , Kong L , Wang S , Liu Z , Wei L , He Y , Wang J , Zhang X .

 

Nat Commun. 2018 Dec 14;9(1):5326. doi: 10.1038/s41467-018-07704-x.

 

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.

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