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Genomic mutations and changes in protein secondary structure and solvent accessibility of SARS-CoV-2 (COVID-19 virus)

Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is a highly pathogenic virus that has caused the global COVID-19 pandemic. Tracing the evolution and transmission of the virus is crucial to respond to and control the pandemic through appropriate intervention strategies. This paper report...

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Autores principales: Nguyen, Thanh Thi, Pathirana, Pubudu N., Nguyen, Thin, Nguyen, Quoc Viet Hung, Bhatti, Asim, Nguyen, Dinh C., Nguyen, Dung Tien, Nguyen, Ngoc Duy, Creighton, Douglas, Abdelrazek, Mohamed
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7876117/
https://www.ncbi.nlm.nih.gov/pubmed/33568759
http://dx.doi.org/10.1038/s41598-021-83105-3
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author Nguyen, Thanh Thi
Pathirana, Pubudu N.
Nguyen, Thin
Nguyen, Quoc Viet Hung
Bhatti, Asim
Nguyen, Dinh C.
Nguyen, Dung Tien
Nguyen, Ngoc Duy
Creighton, Douglas
Abdelrazek, Mohamed
author_facet Nguyen, Thanh Thi
Pathirana, Pubudu N.
Nguyen, Thin
Nguyen, Quoc Viet Hung
Bhatti, Asim
Nguyen, Dinh C.
Nguyen, Dung Tien
Nguyen, Ngoc Duy
Creighton, Douglas
Abdelrazek, Mohamed
author_sort Nguyen, Thanh Thi
collection PubMed
description Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is a highly pathogenic virus that has caused the global COVID-19 pandemic. Tracing the evolution and transmission of the virus is crucial to respond to and control the pandemic through appropriate intervention strategies. This paper reports and analyses genomic mutations in the coding regions of SARS-CoV-2 and their probable protein secondary structure and solvent accessibility changes, which are predicted using deep learning models. Prediction results suggest that mutation D614G in the virus spike protein, which has attracted much attention from researchers, is unlikely to make changes in protein secondary structure and relative solvent accessibility. Based on 6324 viral genome sequences, we create a spreadsheet dataset of point mutations that can facilitate the investigation of SARS-CoV-2 in many perspectives, especially in tracing the evolution and worldwide spread of the virus. Our analysis results also show that coding genes E, M, ORF6, ORF7a, ORF7b and ORF10 are most stable, potentially suitable to be targeted for vaccine and drug development.
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spelling pubmed-78761172021-02-11 Genomic mutations and changes in protein secondary structure and solvent accessibility of SARS-CoV-2 (COVID-19 virus) Nguyen, Thanh Thi Pathirana, Pubudu N. Nguyen, Thin Nguyen, Quoc Viet Hung Bhatti, Asim Nguyen, Dinh C. Nguyen, Dung Tien Nguyen, Ngoc Duy Creighton, Douglas Abdelrazek, Mohamed Sci Rep Article Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is a highly pathogenic virus that has caused the global COVID-19 pandemic. Tracing the evolution and transmission of the virus is crucial to respond to and control the pandemic through appropriate intervention strategies. This paper reports and analyses genomic mutations in the coding regions of SARS-CoV-2 and their probable protein secondary structure and solvent accessibility changes, which are predicted using deep learning models. Prediction results suggest that mutation D614G in the virus spike protein, which has attracted much attention from researchers, is unlikely to make changes in protein secondary structure and relative solvent accessibility. Based on 6324 viral genome sequences, we create a spreadsheet dataset of point mutations that can facilitate the investigation of SARS-CoV-2 in many perspectives, especially in tracing the evolution and worldwide spread of the virus. Our analysis results also show that coding genes E, M, ORF6, ORF7a, ORF7b and ORF10 are most stable, potentially suitable to be targeted for vaccine and drug development. Nature Publishing Group UK 2021-02-10 /pmc/articles/PMC7876117/ /pubmed/33568759 http://dx.doi.org/10.1038/s41598-021-83105-3 Text en © The Author(s) 2021 Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Article
Nguyen, Thanh Thi
Pathirana, Pubudu N.
Nguyen, Thin
Nguyen, Quoc Viet Hung
Bhatti, Asim
Nguyen, Dinh C.
Nguyen, Dung Tien
Nguyen, Ngoc Duy
Creighton, Douglas
Abdelrazek, Mohamed
Genomic mutations and changes in protein secondary structure and solvent accessibility of SARS-CoV-2 (COVID-19 virus)
title Genomic mutations and changes in protein secondary structure and solvent accessibility of SARS-CoV-2 (COVID-19 virus)
title_full Genomic mutations and changes in protein secondary structure and solvent accessibility of SARS-CoV-2 (COVID-19 virus)
title_fullStr Genomic mutations and changes in protein secondary structure and solvent accessibility of SARS-CoV-2 (COVID-19 virus)
title_full_unstemmed Genomic mutations and changes in protein secondary structure and solvent accessibility of SARS-CoV-2 (COVID-19 virus)
title_short Genomic mutations and changes in protein secondary structure and solvent accessibility of SARS-CoV-2 (COVID-19 virus)
title_sort genomic mutations and changes in protein secondary structure and solvent accessibility of sars-cov-2 (covid-19 virus)
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7876117/
https://www.ncbi.nlm.nih.gov/pubmed/33568759
http://dx.doi.org/10.1038/s41598-021-83105-3
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