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In situ architecture and membrane fusion of SARS-CoV-2 Delta variant

Among the current five Variants of Concern, infections caused by SARS-CoV-2 B.1.617.2 (Delta) variant are often associated with the greatest severity. Despite recent advances on the molecular basis of elevated pathogenicity using recombinant proteins, the architecture of intact Delta virions remains...

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Autores principales: Song, Yutong, Yao, Hangping, Wu, Nanping, Xu, Jialu, Zhang, Zheyuan, Peng, Cheng, Li, Shibo, Kong, Weizheng, Chen, Yong, Zhu, Miaojin, Wang, Jiaqi, Shi, Danrong, Zhao, Chongchong, Lu, Xiangyun, Echavarría Galindo, Martín, Li, Sai
Formato: Online Artículo Texto
Lenguaje:English
Publicado: National Academy of Sciences 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10160983/
https://www.ncbi.nlm.nih.gov/pubmed/37094167
http://dx.doi.org/10.1073/pnas.2213332120
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author Song, Yutong
Yao, Hangping
Wu, Nanping
Xu, Jialu
Zhang, Zheyuan
Peng, Cheng
Li, Shibo
Kong, Weizheng
Chen, Yong
Zhu, Miaojin
Wang, Jiaqi
Shi, Danrong
Zhao, Chongchong
Lu, Xiangyun
Echavarría Galindo, Martín
Li, Sai
author_facet Song, Yutong
Yao, Hangping
Wu, Nanping
Xu, Jialu
Zhang, Zheyuan
Peng, Cheng
Li, Shibo
Kong, Weizheng
Chen, Yong
Zhu, Miaojin
Wang, Jiaqi
Shi, Danrong
Zhao, Chongchong
Lu, Xiangyun
Echavarría Galindo, Martín
Li, Sai
author_sort Song, Yutong
collection PubMed
description Among the current five Variants of Concern, infections caused by SARS-CoV-2 B.1.617.2 (Delta) variant are often associated with the greatest severity. Despite recent advances on the molecular basis of elevated pathogenicity using recombinant proteins, the architecture of intact Delta virions remains veiled. Moreover, pieces of molecular evidence for the detailed mechanism of S-mediated membrane fusion are missing. Here, we showed the pleomorphic nature of Delta virions from electron beam inactivated samples and reported the in situ structure and distribution of S on the authentic Delta variant. We also captured the virus–virus fusion events, which provided pieces of structural evidence for Delta’s attenuated dependency on cellular factors for fusion activation, and proposed a model of S-mediated membrane fusion. Besides, site-specific glycan analysis revealed increased oligomannose-type glycosylation of native Delta S than that of the WT S. Together, these results disclose distinctive factors of Delta being the most virulent SARS-CoV-2 variant.
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spelling pubmed-101609832023-05-06 In situ architecture and membrane fusion of SARS-CoV-2 Delta variant Song, Yutong Yao, Hangping Wu, Nanping Xu, Jialu Zhang, Zheyuan Peng, Cheng Li, Shibo Kong, Weizheng Chen, Yong Zhu, Miaojin Wang, Jiaqi Shi, Danrong Zhao, Chongchong Lu, Xiangyun Echavarría Galindo, Martín Li, Sai Proc Natl Acad Sci U S A Biological Sciences Among the current five Variants of Concern, infections caused by SARS-CoV-2 B.1.617.2 (Delta) variant are often associated with the greatest severity. Despite recent advances on the molecular basis of elevated pathogenicity using recombinant proteins, the architecture of intact Delta virions remains veiled. Moreover, pieces of molecular evidence for the detailed mechanism of S-mediated membrane fusion are missing. Here, we showed the pleomorphic nature of Delta virions from electron beam inactivated samples and reported the in situ structure and distribution of S on the authentic Delta variant. We also captured the virus–virus fusion events, which provided pieces of structural evidence for Delta’s attenuated dependency on cellular factors for fusion activation, and proposed a model of S-mediated membrane fusion. Besides, site-specific glycan analysis revealed increased oligomannose-type glycosylation of native Delta S than that of the WT S. Together, these results disclose distinctive factors of Delta being the most virulent SARS-CoV-2 variant. National Academy of Sciences 2023-04-24 2023-05-02 /pmc/articles/PMC10160983/ /pubmed/37094167 http://dx.doi.org/10.1073/pnas.2213332120 Text en Copyright © 2023 the Author(s). Published by PNAS. https://creativecommons.org/licenses/by-nc-nd/4.0/This open access article is distributed under Creative Commons Attribution-NonCommercial-NoDerivatives License 4.0 (CC BY-NC-ND) (https://creativecommons.org/licenses/by-nc-nd/4.0/) .
spellingShingle Biological Sciences
Song, Yutong
Yao, Hangping
Wu, Nanping
Xu, Jialu
Zhang, Zheyuan
Peng, Cheng
Li, Shibo
Kong, Weizheng
Chen, Yong
Zhu, Miaojin
Wang, Jiaqi
Shi, Danrong
Zhao, Chongchong
Lu, Xiangyun
Echavarría Galindo, Martín
Li, Sai
In situ architecture and membrane fusion of SARS-CoV-2 Delta variant
title In situ architecture and membrane fusion of SARS-CoV-2 Delta variant
title_full In situ architecture and membrane fusion of SARS-CoV-2 Delta variant
title_fullStr In situ architecture and membrane fusion of SARS-CoV-2 Delta variant
title_full_unstemmed In situ architecture and membrane fusion of SARS-CoV-2 Delta variant
title_short In situ architecture and membrane fusion of SARS-CoV-2 Delta variant
title_sort in situ architecture and membrane fusion of sars-cov-2 delta variant
topic Biological Sciences
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10160983/
https://www.ncbi.nlm.nih.gov/pubmed/37094167
http://dx.doi.org/10.1073/pnas.2213332120
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