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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Nature Portfolio
2021
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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) |
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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 |
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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 |
_version_ |
1718429210360414208 |