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...
Main Authors: | , , , , , , , , , , , , |
---|---|
Format: | Article |
Language: | English |
Published: |
Nature Portfolio
2018-12-01
|
Series: | Nature Communications |
Online Access: | https://doi.org/10.1038/s41467-018-07704-x |
_version_ | 1819039773321330688 |
---|---|
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. |
first_indexed | 2024-12-21T08:58:32Z |
format | Article |
id | doaj.art-b7ce35978c4040f9bd16bfeabee93ecf |
institution | Directory Open Access Journal |
issn | 2041-1723 |
language | English |
last_indexed | 2024-12-21T08:58:32Z |
publishDate | 2018-12-01 |
publisher | Nature Portfolio |
record_format | Article |
series | Nature Communications |
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 |
work_keys_str_mv | AT lihongchen implicationforalphavirushostcellentryandassemblyindicatedbya35aresolutioncryoemstructure AT mingwang implicationforalphavirushostcellentryandassemblyindicatedbya35aresolutioncryoemstructure AT dongjiezhu implicationforalphavirushostcellentryandassemblyindicatedbya35aresolutioncryoemstructure AT zhenzhaosun implicationforalphavirushostcellentryandassemblyindicatedbya35aresolutioncryoemstructure AT junma implicationforalphavirushostcellentryandassemblyindicatedbya35aresolutioncryoemstructure AT jinglinwang implicationforalphavirushostcellentryandassemblyindicatedbya35aresolutioncryoemstructure AT lingfeikong implicationforalphavirushostcellentryandassemblyindicatedbya35aresolutioncryoemstructure AT shidawang implicationforalphavirushostcellentryandassemblyindicatedbya35aresolutioncryoemstructure AT zaisiliu implicationforalphavirushostcellentryandassemblyindicatedbya35aresolutioncryoemstructure AT liliwei implicationforalphavirushostcellentryandassemblyindicatedbya35aresolutioncryoemstructure AT yuwenhe implicationforalphavirushostcellentryandassemblyindicatedbya35aresolutioncryoemstructure AT jingfeiwang implicationforalphavirushostcellentryandassemblyindicatedbya35aresolutioncryoemstructure AT xinzhengzhang implicationforalphavirushostcellentryandassemblyindicatedbya35aresolutioncryoemstructure |