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Structural Insights into Alphavirus Assembly Revealed by the Cryo-EM Structure of Getah Virus
Getah virus (GETV) is a member of the alphavirus genus, and it infects a variety of animal species, including horses, pigs, cattle, and foxes. Human infection with this virus has also been reported. The structure of GETV has not yet been determined. In this study, we report the cryo-EM structure of...
Autores principales: | , , , , , , , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8876998/ https://www.ncbi.nlm.nih.gov/pubmed/35215918 http://dx.doi.org/10.3390/v14020327 |
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author | Wang, Ming Sun, Zhenzhao Cui, Chenxi Wang, Shida Yang, Decheng Shi, Zhibin Wei, Xinyu Wang, Pengfei Sun, Weiyao Zhu, Jing Li, Jiaqi Du, Bingchen Liu, Zaisi Wei, Lili Liu, Chunguo He, Xijun Wang, Xiangxi Zhang, Xinzheng Wang, Jingfei |
author_facet | Wang, Ming Sun, Zhenzhao Cui, Chenxi Wang, Shida Yang, Decheng Shi, Zhibin Wei, Xinyu Wang, Pengfei Sun, Weiyao Zhu, Jing Li, Jiaqi Du, Bingchen Liu, Zaisi Wei, Lili Liu, Chunguo He, Xijun Wang, Xiangxi Zhang, Xinzheng Wang, Jingfei |
author_sort | Wang, Ming |
collection | PubMed |
description | Getah virus (GETV) is a member of the alphavirus genus, and it infects a variety of animal species, including horses, pigs, cattle, and foxes. Human infection with this virus has also been reported. The structure of GETV has not yet been determined. In this study, we report the cryo-EM structure of GETV at a resolution of 3.5 Å. This structure reveals conformational polymorphism of the envelope glycoproteins E1 and E2 at icosahedral 3-fold and quasi-3-fold axes, which is believed to be a necessary organization in forming a curvature surface of virions. In our density map, three extra densities are identified, one of which is believed a “pocket factor”; the other two are located by domain D of E2, and they may maintain the stability of E1/E2 heterodimers. We also identify three N-glycosylations at E1 N141, E2 N200, and E2 N262, which might be associated with receptor binding and membrane fusion. The resolving of the structure of GETV provides new insights into the structure and assembly of alphaviruses and lays a basis for studying the differences of biology and pathogenicity between arthritogenic and encephalitic alphaviruses. |
format | Online Article Text |
id | pubmed-8876998 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-88769982022-02-26 Structural Insights into Alphavirus Assembly Revealed by the Cryo-EM Structure of Getah Virus Wang, Ming Sun, Zhenzhao Cui, Chenxi Wang, Shida Yang, Decheng Shi, Zhibin Wei, Xinyu Wang, Pengfei Sun, Weiyao Zhu, Jing Li, Jiaqi Du, Bingchen Liu, Zaisi Wei, Lili Liu, Chunguo He, Xijun Wang, Xiangxi Zhang, Xinzheng Wang, Jingfei Viruses Article Getah virus (GETV) is a member of the alphavirus genus, and it infects a variety of animal species, including horses, pigs, cattle, and foxes. Human infection with this virus has also been reported. The structure of GETV has not yet been determined. In this study, we report the cryo-EM structure of GETV at a resolution of 3.5 Å. This structure reveals conformational polymorphism of the envelope glycoproteins E1 and E2 at icosahedral 3-fold and quasi-3-fold axes, which is believed to be a necessary organization in forming a curvature surface of virions. In our density map, three extra densities are identified, one of which is believed a “pocket factor”; the other two are located by domain D of E2, and they may maintain the stability of E1/E2 heterodimers. We also identify three N-glycosylations at E1 N141, E2 N200, and E2 N262, which might be associated with receptor binding and membrane fusion. The resolving of the structure of GETV provides new insights into the structure and assembly of alphaviruses and lays a basis for studying the differences of biology and pathogenicity between arthritogenic and encephalitic alphaviruses. MDPI 2022-02-05 /pmc/articles/PMC8876998/ /pubmed/35215918 http://dx.doi.org/10.3390/v14020327 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Wang, Ming Sun, Zhenzhao Cui, Chenxi Wang, Shida Yang, Decheng Shi, Zhibin Wei, Xinyu Wang, Pengfei Sun, Weiyao Zhu, Jing Li, Jiaqi Du, Bingchen Liu, Zaisi Wei, Lili Liu, Chunguo He, Xijun Wang, Xiangxi Zhang, Xinzheng Wang, Jingfei Structural Insights into Alphavirus Assembly Revealed by the Cryo-EM Structure of Getah Virus |
title | Structural Insights into Alphavirus Assembly Revealed by the Cryo-EM Structure of Getah Virus |
title_full | Structural Insights into Alphavirus Assembly Revealed by the Cryo-EM Structure of Getah Virus |
title_fullStr | Structural Insights into Alphavirus Assembly Revealed by the Cryo-EM Structure of Getah Virus |
title_full_unstemmed | Structural Insights into Alphavirus Assembly Revealed by the Cryo-EM Structure of Getah Virus |
title_short | Structural Insights into Alphavirus Assembly Revealed by the Cryo-EM Structure of Getah Virus |
title_sort | structural insights into alphavirus assembly revealed by the cryo-em structure of getah virus |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8876998/ https://www.ncbi.nlm.nih.gov/pubmed/35215918 http://dx.doi.org/10.3390/v14020327 |
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