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

Alphaviruses are enveloped RNA viruses that contain several human pathogens. Here, the authors use block-based reconstruction method and provide a 3.5 Å cryo-EM structure of sindbis virus that identifies a conserved hydrophobic pocket near the viral membrane that is stabilized by an unknown pocket f...

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Main Authors: 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
Format: Article
Language:English
Published: Nature Portfolio 2018-12-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-018-07704-x
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author 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
author_facet 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
author_sort Lihong Chen
collection DOAJ
description Alphaviruses are enveloped RNA viruses that contain several human pathogens. Here, the authors use block-based reconstruction method and provide a 3.5 Å cryo-EM structure of sindbis virus that identifies a conserved hydrophobic pocket near the viral membrane that is stabilized by an unknown pocket factor.
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spelling doaj.art-b7ce35978c4040f9bd16bfeabee93ecf2022-12-21T19:09:31ZengNature PortfolioNature Communications2041-17232018-12-01911810.1038/s41467-018-07704-xImplication for alphavirus host-cell entry and assembly indicated by a 3.5Å resolution cryo-EM structureLihong Chen0Ming Wang1Dongjie Zhu2Zhenzhao Sun3Jun Ma4Jinglin Wang5Lingfei Kong6Shida Wang7Zaisi Liu8Lili Wei9Yuwen He10Jingfei Wang11Xinzheng Zhang12National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of SciencesState Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute, Chinese Academy of Agricultural SciencesNational Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of SciencesState Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute, Chinese Academy of Agricultural SciencesNational Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of SciencesYunnan Tropical and Subtropical Animal Viral Disease Laboratory, Yunnan Animal Science and Veterinary InstituteNational Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of SciencesState Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute, Chinese Academy of Agricultural SciencesState Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute, Chinese Academy of Agricultural SciencesState Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute, Chinese Academy of Agricultural SciencesYunnan Tropical and Subtropical Animal Viral Disease Laboratory, Yunnan Animal Science and Veterinary InstituteState Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute, Chinese Academy of Agricultural SciencesNational Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of SciencesAlphaviruses are enveloped RNA viruses that contain several human pathogens. Here, the authors use block-based reconstruction method and provide a 3.5 Å cryo-EM structure of sindbis virus that identifies a conserved hydrophobic pocket near the viral membrane that is stabilized by an unknown pocket factor.https://doi.org/10.1038/s41467-018-07704-x
spellingShingle 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
Implication for alphavirus host-cell entry and assembly indicated by a 3.5Å resolution cryo-EM structure
Nature Communications
title Implication for alphavirus host-cell entry and assembly indicated by a 3.5Å resolution cryo-EM structure
title_full Implication for alphavirus host-cell entry and assembly indicated by a 3.5Å resolution cryo-EM structure
title_fullStr Implication for alphavirus host-cell entry and assembly indicated by a 3.5Å resolution cryo-EM structure
title_full_unstemmed Implication for alphavirus host-cell entry and assembly indicated by a 3.5Å resolution cryo-EM structure
title_short Implication for alphavirus host-cell entry and assembly indicated by a 3.5Å resolution cryo-EM structure
title_sort implication for alphavirus host cell entry and assembly indicated by a 3 5a resolution cryo em structure
url https://doi.org/10.1038/s41467-018-07704-x
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