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Rapid Degradation of SARS-CoV-2 Spike S Protein by A Specific Serine Protease

The S protein of SARS-CoV-2 is a crucial structural and functional component for virus entry. Due to the constant mutation of the virus, there are very limited ways to prevent and control COVID-19. This experiment used a macroscopic SDS-PAGE method and proved that the S protein of wild-type SARS-CoV...

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Autores principales: Liu, Jiankai, Kan, Mujie, Zhang, Lianzhi, Yue, Yuan, Wang, Shaohua, Hong, Min, Hong, Xinyu
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8954242/
https://www.ncbi.nlm.nih.gov/pubmed/35335246
http://dx.doi.org/10.3390/molecules27061882
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author Liu, Jiankai
Kan, Mujie
Zhang, Lianzhi
Yue, Yuan
Wang, Shaohua
Hong, Min
Hong, Xinyu
author_facet Liu, Jiankai
Kan, Mujie
Zhang, Lianzhi
Yue, Yuan
Wang, Shaohua
Hong, Min
Hong, Xinyu
author_sort Liu, Jiankai
collection PubMed
description The S protein of SARS-CoV-2 is a crucial structural and functional component for virus entry. Due to the constant mutation of the virus, there are very limited ways to prevent and control COVID-19. This experiment used a macroscopic SDS-PAGE method and proved that the S protein of wild-type SARS-CoV-2 virus, especially the S1 subunit, is very sensitive to alkaline serine protease with acidic pI (ASPNJ), NJ represents Neanthes japonica (Izuka) from which ASP is purified). ASPNJ cleaves proteins when the carbonyl group of the peptide bond is contributed by arginine or lysine. ASPNJ can degrade the S protein very quickly and effectively in vitro with relative selectivity. It can be inferred that the S, S1 and RBD of SARS-CoV-2 variants can also be easily degraded by ASPNJ. This rapid and strong degradation of the S protein by ASPNJ may become a potential new treatment strategy.
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spelling pubmed-89542422022-03-26 Rapid Degradation of SARS-CoV-2 Spike S Protein by A Specific Serine Protease Liu, Jiankai Kan, Mujie Zhang, Lianzhi Yue, Yuan Wang, Shaohua Hong, Min Hong, Xinyu Molecules Article The S protein of SARS-CoV-2 is a crucial structural and functional component for virus entry. Due to the constant mutation of the virus, there are very limited ways to prevent and control COVID-19. This experiment used a macroscopic SDS-PAGE method and proved that the S protein of wild-type SARS-CoV-2 virus, especially the S1 subunit, is very sensitive to alkaline serine protease with acidic pI (ASPNJ), NJ represents Neanthes japonica (Izuka) from which ASP is purified). ASPNJ cleaves proteins when the carbonyl group of the peptide bond is contributed by arginine or lysine. ASPNJ can degrade the S protein very quickly and effectively in vitro with relative selectivity. It can be inferred that the S, S1 and RBD of SARS-CoV-2 variants can also be easily degraded by ASPNJ. This rapid and strong degradation of the S protein by ASPNJ may become a potential new treatment strategy. MDPI 2022-03-14 /pmc/articles/PMC8954242/ /pubmed/35335246 http://dx.doi.org/10.3390/molecules27061882 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Liu, Jiankai
Kan, Mujie
Zhang, Lianzhi
Yue, Yuan
Wang, Shaohua
Hong, Min
Hong, Xinyu
Rapid Degradation of SARS-CoV-2 Spike S Protein by A Specific Serine Protease
title Rapid Degradation of SARS-CoV-2 Spike S Protein by A Specific Serine Protease
title_full Rapid Degradation of SARS-CoV-2 Spike S Protein by A Specific Serine Protease
title_fullStr Rapid Degradation of SARS-CoV-2 Spike S Protein by A Specific Serine Protease
title_full_unstemmed Rapid Degradation of SARS-CoV-2 Spike S Protein by A Specific Serine Protease
title_short Rapid Degradation of SARS-CoV-2 Spike S Protein by A Specific Serine Protease
title_sort rapid degradation of sars-cov-2 spike s protein by a specific serine protease
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8954242/
https://www.ncbi.nlm.nih.gov/pubmed/35335246
http://dx.doi.org/10.3390/molecules27061882
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