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Reasoning of spike glycoproteins being more vulnerable to mutations among 158 coronavirus proteins from different species
In this study, we used the probabilistic models developed by us over the last several years to analyze 158 proteins from coronaviruses in order to determine which protein is more vulnerable to mutations. The results provide three lines of evidence suggesting that the spike glycoprotein is different...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer-Verlag
2004
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7088192/ https://www.ncbi.nlm.nih.gov/pubmed/15592899 http://dx.doi.org/10.1007/s00894-004-0210-0 |
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author | Wu, Guang Yan, Shaomin |
author_facet | Wu, Guang Yan, Shaomin |
author_sort | Wu, Guang |
collection | PubMed |
description | In this study, we used the probabilistic models developed by us over the last several years to analyze 158 proteins from coronaviruses in order to determine which protein is more vulnerable to mutations. The results provide three lines of evidence suggesting that the spike glycoprotein is different from the other coronavirus proteins: (1) the spike glycoprotein is more sensitive to mutations, this is the current state of the spike glycoprotein, (2) the spike glycoprotein has undergone more mutations in the past, this is the history of spike glycoprotein, and (3) the spike glycoprotein has a bigger potential towards future mutations, this is the future of spike glycoprotein. Furthermore, this study gives a clue on the species susceptibility regarding different proteins. Figure Predictable and unpredictable portions in coronavirus proteins. The data are presented as median with interquartile range. * the predictable and unpredictable portions in spike glycoprotein group are statistically different from any other protein groups at p<0.05 level, except for hemagglutinin-esterase precursor group. # the predictable and unpredictable portions in spike glycoprotein group are statistically different from hemagglutinin-esterase precursor, membrane protein and nucleocapsid protein groups at p<0.05 level. † the predictable and unpredictable portions in spike glycoprotein group are statistically different from hemagglutinin-esterase precursor, and membrane protein groups at p<0.05 level. Electronic Supplementary Material is available for this article if you access the article at http://dx.doi.org/10.1007/s00894-004-0210-0. |
format | Online Article Text |
id | pubmed-7088192 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2004 |
publisher | Springer-Verlag |
record_format | MEDLINE/PubMed |
spelling | pubmed-70881922020-03-23 Reasoning of spike glycoproteins being more vulnerable to mutations among 158 coronavirus proteins from different species Wu, Guang Yan, Shaomin J Mol Model Original Paper In this study, we used the probabilistic models developed by us over the last several years to analyze 158 proteins from coronaviruses in order to determine which protein is more vulnerable to mutations. The results provide three lines of evidence suggesting that the spike glycoprotein is different from the other coronavirus proteins: (1) the spike glycoprotein is more sensitive to mutations, this is the current state of the spike glycoprotein, (2) the spike glycoprotein has undergone more mutations in the past, this is the history of spike glycoprotein, and (3) the spike glycoprotein has a bigger potential towards future mutations, this is the future of spike glycoprotein. Furthermore, this study gives a clue on the species susceptibility regarding different proteins. Figure Predictable and unpredictable portions in coronavirus proteins. The data are presented as median with interquartile range. * the predictable and unpredictable portions in spike glycoprotein group are statistically different from any other protein groups at p<0.05 level, except for hemagglutinin-esterase precursor group. # the predictable and unpredictable portions in spike glycoprotein group are statistically different from hemagglutinin-esterase precursor, membrane protein and nucleocapsid protein groups at p<0.05 level. † the predictable and unpredictable portions in spike glycoprotein group are statistically different from hemagglutinin-esterase precursor, and membrane protein groups at p<0.05 level. Electronic Supplementary Material is available for this article if you access the article at http://dx.doi.org/10.1007/s00894-004-0210-0. Springer-Verlag 2004-12-09 2005 /pmc/articles/PMC7088192/ /pubmed/15592899 http://dx.doi.org/10.1007/s00894-004-0210-0 Text en © Springer-Verlag 2004 This article is made available via the PMC Open Access Subset for unrestricted research re-use and secondary analysis in any form or by any means with acknowledgement of the original source. These permissions are granted for the duration of the World Health Organization (WHO) declaration of COVID-19 as a global pandemic. |
spellingShingle | Original Paper Wu, Guang Yan, Shaomin Reasoning of spike glycoproteins being more vulnerable to mutations among 158 coronavirus proteins from different species |
title | Reasoning of spike glycoproteins being more vulnerable to mutations among 158 coronavirus proteins from different species |
title_full | Reasoning of spike glycoproteins being more vulnerable to mutations among 158 coronavirus proteins from different species |
title_fullStr | Reasoning of spike glycoproteins being more vulnerable to mutations among 158 coronavirus proteins from different species |
title_full_unstemmed | Reasoning of spike glycoproteins being more vulnerable to mutations among 158 coronavirus proteins from different species |
title_short | Reasoning of spike glycoproteins being more vulnerable to mutations among 158 coronavirus proteins from different species |
title_sort | reasoning of spike glycoproteins being more vulnerable to mutations among 158 coronavirus proteins from different species |
topic | Original Paper |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7088192/ https://www.ncbi.nlm.nih.gov/pubmed/15592899 http://dx.doi.org/10.1007/s00894-004-0210-0 |
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