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CryoEM structure of the tegumented capsid of Epstein-Barr virus
Epstein-Barr virus (EBV) is the primary cause of infectious mononucleosis and has been shown to be closely associated with various malignancies. Here, we present a complete atomic model of EBV, including the icosahedral capsid, the dodecameric portal and the capsid-associated tegument complex (CATC)...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer Singapore
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7608217/ https://www.ncbi.nlm.nih.gov/pubmed/32620850 http://dx.doi.org/10.1038/s41422-020-0363-0 |
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author | Li, Zhihai Zhang, Xiao Dong, Lili Pang, Jingjing Xu, Miao Zhong, Qian Zeng, Mu-Sheng Yu, Xuekui |
author_facet | Li, Zhihai Zhang, Xiao Dong, Lili Pang, Jingjing Xu, Miao Zhong, Qian Zeng, Mu-Sheng Yu, Xuekui |
author_sort | Li, Zhihai |
collection | PubMed |
description | Epstein-Barr virus (EBV) is the primary cause of infectious mononucleosis and has been shown to be closely associated with various malignancies. Here, we present a complete atomic model of EBV, including the icosahedral capsid, the dodecameric portal and the capsid-associated tegument complex (CATC). Our in situ portal from the tegumented capsid adopts a closed conformation with its channel valve holding the terminal viral DNA and with its crown region firmly engaged by three layers of ring-like dsDNA, which, together with the penton flexibility, effectively alleviates the capsid inner pressure placed on the portal cap. In contrast, the CATCs, through binding to the flexible penton vertices in a stoichiometric manner, accurately increase the inner capsid pressure to facilitate the pressure-driven genome delivery. Together, our results provide important insights into the mechanism by which the EBV capsid, portal, packaged genome and the CATCs coordinately achieve a pressure balance to simultaneously benefit both viral genome retention and ejection. |
format | Online Article Text |
id | pubmed-7608217 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Springer Singapore |
record_format | MEDLINE/PubMed |
spelling | pubmed-76082172020-11-05 CryoEM structure of the tegumented capsid of Epstein-Barr virus Li, Zhihai Zhang, Xiao Dong, Lili Pang, Jingjing Xu, Miao Zhong, Qian Zeng, Mu-Sheng Yu, Xuekui Cell Res Article Epstein-Barr virus (EBV) is the primary cause of infectious mononucleosis and has been shown to be closely associated with various malignancies. Here, we present a complete atomic model of EBV, including the icosahedral capsid, the dodecameric portal and the capsid-associated tegument complex (CATC). Our in situ portal from the tegumented capsid adopts a closed conformation with its channel valve holding the terminal viral DNA and with its crown region firmly engaged by three layers of ring-like dsDNA, which, together with the penton flexibility, effectively alleviates the capsid inner pressure placed on the portal cap. In contrast, the CATCs, through binding to the flexible penton vertices in a stoichiometric manner, accurately increase the inner capsid pressure to facilitate the pressure-driven genome delivery. Together, our results provide important insights into the mechanism by which the EBV capsid, portal, packaged genome and the CATCs coordinately achieve a pressure balance to simultaneously benefit both viral genome retention and ejection. Springer Singapore 2020-07-03 2020-10 /pmc/articles/PMC7608217/ /pubmed/32620850 http://dx.doi.org/10.1038/s41422-020-0363-0 Text en © The Author(s) 2020 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Li, Zhihai Zhang, Xiao Dong, Lili Pang, Jingjing Xu, Miao Zhong, Qian Zeng, Mu-Sheng Yu, Xuekui CryoEM structure of the tegumented capsid of Epstein-Barr virus |
title | CryoEM structure of the tegumented capsid of Epstein-Barr virus |
title_full | CryoEM structure of the tegumented capsid of Epstein-Barr virus |
title_fullStr | CryoEM structure of the tegumented capsid of Epstein-Barr virus |
title_full_unstemmed | CryoEM structure of the tegumented capsid of Epstein-Barr virus |
title_short | CryoEM structure of the tegumented capsid of Epstein-Barr virus |
title_sort | cryoem structure of the tegumented capsid of epstein-barr virus |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7608217/ https://www.ncbi.nlm.nih.gov/pubmed/32620850 http://dx.doi.org/10.1038/s41422-020-0363-0 |
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