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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)...

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Autores principales: Li, Zhihai, Zhang, Xiao, Dong, Lili, Pang, Jingjing, Xu, Miao, Zhong, Qian, Zeng, Mu-Sheng, Yu, Xuekui
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Singapore 2020
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.
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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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