Implication for alphavirus host-cell entry and assembly indicated by a 3.5 angstrom resolution cryo-EM structure, Nat Commun, 14 Dec 2018
发布时间：2018年12月14日
Nature Communications, 14 December 2018
Implication for alphavirus host-cell entry and assembly indicated by a 3.5 angstrom 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 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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Implication for alphavirus host-cell entry and assembly indicated by a 3.5 angstrom resolution cryo-EM structure, Nat Commun, 14 Dec 2018
Nature Communications, 14 December 2018
Implication for alphavirus host-cell entry and assembly indicated by a 3.5 angstrom 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 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.
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