Exposing structural variations in SARS-CoV-2 evolution

Abstract The mutation of SARS-CoV-2 influences viral function as residue replacements affect both physiochemical properties and folding conformations. Although a large amount of data on SARS-CoV-2 is available, the investigation of how viral functions change in response to mutations is hampered by a...

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Autores principales: Jiaan Yang, Peng Zhang, Wen Xiang Cheng, Youyong Lu, Wu Gang, Gang Ren
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Lenguaje:EN
Publicado: Nature Portfolio 2021
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Acceso en línea:https://doaj.org/article/0908003be58742d496ceb07d73b80cc1
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spelling oai:doaj.org-article:0908003be58742d496ceb07d73b80cc12021-11-14T12:21:11ZExposing structural variations in SARS-CoV-2 evolution10.1038/s41598-021-01650-32045-2322https://doaj.org/article/0908003be58742d496ceb07d73b80cc12021-11-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-01650-3https://doaj.org/toc/2045-2322Abstract The mutation of SARS-CoV-2 influences viral function as residue replacements affect both physiochemical properties and folding conformations. Although a large amount of data on SARS-CoV-2 is available, the investigation of how viral functions change in response to mutations is hampered by a lack of effective structural analysis. Here, we exploit the advances of protein structure fingerprint technology to study the folding conformational changes induced by mutations. With integration of both protein sequences and folding conformations, the structures are aligned for SARS-CoV to SARS-CoV-2, including Alpha variant (lineage B.1.1.7) and Delta variant (lineage B.1.617.2). The results showed that the virus evolution with change in mutational positions and physicochemical properties increased the affinity between spike protein and ACE2, which plays a critical role in coronavirus entry into human cells. Additionally, these structural variations impact vaccine effectiveness and drug function over the course of SARS-CoV-2 evolution. The analysis of structural variations revealed how the coronavirus has gradually evolved in both structure and function and how the SARS-CoV-2 variants have contributed to more severe acute disease worldwide.Jiaan YangPeng ZhangWen Xiang ChengYouyong LuWu GangGang RenNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-14 (2021)
institution DOAJ
collection DOAJ
language EN
topic Medicine
R
Science
Q
spellingShingle Medicine
R
Science
Q
Jiaan Yang
Peng Zhang
Wen Xiang Cheng
Youyong Lu
Wu Gang
Gang Ren
Exposing structural variations in SARS-CoV-2 evolution
description Abstract The mutation of SARS-CoV-2 influences viral function as residue replacements affect both physiochemical properties and folding conformations. Although a large amount of data on SARS-CoV-2 is available, the investigation of how viral functions change in response to mutations is hampered by a lack of effective structural analysis. Here, we exploit the advances of protein structure fingerprint technology to study the folding conformational changes induced by mutations. With integration of both protein sequences and folding conformations, the structures are aligned for SARS-CoV to SARS-CoV-2, including Alpha variant (lineage B.1.1.7) and Delta variant (lineage B.1.617.2). The results showed that the virus evolution with change in mutational positions and physicochemical properties increased the affinity between spike protein and ACE2, which plays a critical role in coronavirus entry into human cells. Additionally, these structural variations impact vaccine effectiveness and drug function over the course of SARS-CoV-2 evolution. The analysis of structural variations revealed how the coronavirus has gradually evolved in both structure and function and how the SARS-CoV-2 variants have contributed to more severe acute disease worldwide.
format article
author Jiaan Yang
Peng Zhang
Wen Xiang Cheng
Youyong Lu
Wu Gang
Gang Ren
author_facet Jiaan Yang
Peng Zhang
Wen Xiang Cheng
Youyong Lu
Wu Gang
Gang Ren
author_sort Jiaan Yang
title Exposing structural variations in SARS-CoV-2 evolution
title_short Exposing structural variations in SARS-CoV-2 evolution
title_full Exposing structural variations in SARS-CoV-2 evolution
title_fullStr Exposing structural variations in SARS-CoV-2 evolution
title_full_unstemmed Exposing structural variations in SARS-CoV-2 evolution
title_sort exposing structural variations in sars-cov-2 evolution
publisher Nature Portfolio
publishDate 2021
url https://doaj.org/article/0908003be58742d496ceb07d73b80cc1
work_keys_str_mv AT jiaanyang exposingstructuralvariationsinsarscov2evolution
AT pengzhang exposingstructuralvariationsinsarscov2evolution
AT wenxiangcheng exposingstructuralvariationsinsarscov2evolution
AT youyonglu exposingstructuralvariationsinsarscov2evolution
AT wugang exposingstructuralvariationsinsarscov2evolution
AT gangren exposingstructuralvariationsinsarscov2evolution
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