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SARS-CoV-2 spike protein displays sequence similarities with paramyxovirus surface proteins; a bioinformatics study

Recent emergence of SARS-CoV-2 and associated COVID-19 pandemic have posed a great challenge for the scientific community. In this study, we performed bioinformatic analyses on SARS-CoV-2 protein sequences, trying to unravel potential molecular similarities between this newly emerged pathogen with n...

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Autores principales: Ahmadi, Ehsan, Zabihi, Mohammad Reza, Hosseinzadeh, Ramin, Mohamed Khosroshahi, Leila, Noorbakhsh, Farshid
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8639087/
https://www.ncbi.nlm.nih.gov/pubmed/34855795
http://dx.doi.org/10.1371/journal.pone.0260360
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author Ahmadi, Ehsan
Zabihi, Mohammad Reza
Hosseinzadeh, Ramin
Mohamed Khosroshahi, Leila
Noorbakhsh, Farshid
author_facet Ahmadi, Ehsan
Zabihi, Mohammad Reza
Hosseinzadeh, Ramin
Mohamed Khosroshahi, Leila
Noorbakhsh, Farshid
author_sort Ahmadi, Ehsan
collection PubMed
description Recent emergence of SARS-CoV-2 and associated COVID-19 pandemic have posed a great challenge for the scientific community. In this study, we performed bioinformatic analyses on SARS-CoV-2 protein sequences, trying to unravel potential molecular similarities between this newly emerged pathogen with non-coronavirus ssRNA viruses. Comparing the proteins of SARS-CoV-2 with non-coronavirus positive and negative strand ssRNA viruses revealed multiple sequence similarities between SARS-CoV-2 and non-coronaviruses, including similarities between RNA-dependent RNA-polymerases and helicases (two highly-conserved proteins). We also observed similarities between SARS-CoV-2 surface (i.e. spike) protein with paramyxovirus fusion proteins. This similarity was restricted to a segment of spike protein S2 subunit which is involved in cell fusion. We next analyzed spike proteins from SARS-CoV-2 “variants of concern” (VOCs) and “variants of interests” (VOIs) and found that some of these variants show considerably higher spike-fusion similarity with paramyxoviruses. The ‘spike-fusion’ similarity was also observed for some pathogenic coronaviruses other than SARS-CoV-2. Epitope analysis using experimentally verified data deposited in Immune Epitope Database (IEDB) revealed that several B cell epitopes as well as T cell and MHC binding epitopes map within the spike-fusion similarity region. These data indicate that there might be a degree of convergent evolution between SARS-CoV-2 and paramyxovirus surface proteins which could be of pathogenic and immunological importance.
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spelling pubmed-86390872021-12-03 SARS-CoV-2 spike protein displays sequence similarities with paramyxovirus surface proteins; a bioinformatics study Ahmadi, Ehsan Zabihi, Mohammad Reza Hosseinzadeh, Ramin Mohamed Khosroshahi, Leila Noorbakhsh, Farshid PLoS One Research Article Recent emergence of SARS-CoV-2 and associated COVID-19 pandemic have posed a great challenge for the scientific community. In this study, we performed bioinformatic analyses on SARS-CoV-2 protein sequences, trying to unravel potential molecular similarities between this newly emerged pathogen with non-coronavirus ssRNA viruses. Comparing the proteins of SARS-CoV-2 with non-coronavirus positive and negative strand ssRNA viruses revealed multiple sequence similarities between SARS-CoV-2 and non-coronaviruses, including similarities between RNA-dependent RNA-polymerases and helicases (two highly-conserved proteins). We also observed similarities between SARS-CoV-2 surface (i.e. spike) protein with paramyxovirus fusion proteins. This similarity was restricted to a segment of spike protein S2 subunit which is involved in cell fusion. We next analyzed spike proteins from SARS-CoV-2 “variants of concern” (VOCs) and “variants of interests” (VOIs) and found that some of these variants show considerably higher spike-fusion similarity with paramyxoviruses. The ‘spike-fusion’ similarity was also observed for some pathogenic coronaviruses other than SARS-CoV-2. Epitope analysis using experimentally verified data deposited in Immune Epitope Database (IEDB) revealed that several B cell epitopes as well as T cell and MHC binding epitopes map within the spike-fusion similarity region. These data indicate that there might be a degree of convergent evolution between SARS-CoV-2 and paramyxovirus surface proteins which could be of pathogenic and immunological importance. Public Library of Science 2021-12-02 /pmc/articles/PMC8639087/ /pubmed/34855795 http://dx.doi.org/10.1371/journal.pone.0260360 Text en © 2021 Ahmadi et al https://creativecommons.org/licenses/by/4.0/This is an open access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
spellingShingle Research Article
Ahmadi, Ehsan
Zabihi, Mohammad Reza
Hosseinzadeh, Ramin
Mohamed Khosroshahi, Leila
Noorbakhsh, Farshid
SARS-CoV-2 spike protein displays sequence similarities with paramyxovirus surface proteins; a bioinformatics study
title SARS-CoV-2 spike protein displays sequence similarities with paramyxovirus surface proteins; a bioinformatics study
title_full SARS-CoV-2 spike protein displays sequence similarities with paramyxovirus surface proteins; a bioinformatics study
title_fullStr SARS-CoV-2 spike protein displays sequence similarities with paramyxovirus surface proteins; a bioinformatics study
title_full_unstemmed SARS-CoV-2 spike protein displays sequence similarities with paramyxovirus surface proteins; a bioinformatics study
title_short SARS-CoV-2 spike protein displays sequence similarities with paramyxovirus surface proteins; a bioinformatics study
title_sort sars-cov-2 spike protein displays sequence similarities with paramyxovirus surface proteins; a bioinformatics study
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8639087/
https://www.ncbi.nlm.nih.gov/pubmed/34855795
http://dx.doi.org/10.1371/journal.pone.0260360
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