SARS-CoV-2 and ORF3a: Nonsynonymous Mutations, Functional Domains, and Viral Pathogenesis

ABSTRACT The effect of the rapid accumulation of nonsynonymous mutations on the pathogenesis of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is not yet known. The 3a protein is unique to SARS-CoV and is essential for disease pathogenesis. Our study aimed at determining the nonsynonym...

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Autores principales:	Elio Issa, Georgi Merhi, Balig Panossian, Tamara Salloum, Sima Tokajian
Formato:	article
Lenguaje:	EN
Publicado:	American Society for Microbiology 2020
Materias:	3a protein COVID-19 nonsynonymous mutations ORF3a SARS-CoV-2 Microbiology QR1-502
Acceso en línea:	https://doaj.org/article/17820af1c1a44c23afe10b4f64c46b29
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spelling	oai:doaj.org-article:17820af1c1a44c23afe10b4f64c46b292021-12-02T18:44:38ZSARS-CoV-2 and ORF3a: Nonsynonymous Mutations, Functional Domains, and Viral Pathogenesis10.1128/mSystems.00266-202379-5077https://doaj.org/article/17820af1c1a44c23afe10b4f64c46b292020-06-01T00:00:00Zhttps://journals.asm.org/doi/10.1128/mSystems.00266-20https://doaj.org/toc/2379-5077ABSTRACT The effect of the rapid accumulation of nonsynonymous mutations on the pathogenesis of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is not yet known. The 3a protein is unique to SARS-CoV and is essential for disease pathogenesis. Our study aimed at determining the nonsynonymous mutations in the 3a protein in SARS-CoV-2 and determining and characterizing the protein’s structure and spatial orientation in comparison to those of 3a in SARS-CoV. A total of 51 different nonsynonymous amino acid substitutions were detected in the 3a proteins among 2,782 SARS-CoV-2 strains. We observed microclonality within the ORF3a gene tree defined by nonsynonymous mutations separating the isolates into distinct subpopulations. We detected and identified six functional domains (I to VI) in the SARS-CoV-2 3a protein. The functional domains were linked to virulence, infectivity, ion channel formation, and virus release. Our study showed the importance of conserved functional domains across the species barrier and revealed the possible role of the 3a protein in the viral life cycle. Observations reported in this study merit experimental confirmation. IMPORTANCE At the surge of the coronavirus disease 2019 (COVID-19) pandemic, we detected and identified six functional domains (I to VI) in the SARS-CoV-2 3a protein. Our analysis showed that the functional domains were linked to virulence, infectivity, ion channel formation, and virus release in SARS-CoV-2 3a. Our study also revealed the functional importance of conserved domains across the species barrier. Observations reported in this study merit experimental confirmation.Elio IssaGeorgi MerhiBalig PanossianTamara SalloumSima TokajianAmerican Society for Microbiologyarticle3a proteinCOVID-19nonsynonymous mutationsORF3aSARS-CoV-2MicrobiologyQR1-502ENmSystems, Vol 5, Iss 3 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	3a protein COVID-19 nonsynonymous mutations ORF3a SARS-CoV-2 Microbiology QR1-502
spellingShingle	3a protein COVID-19 nonsynonymous mutations ORF3a SARS-CoV-2 Microbiology QR1-502 Elio Issa Georgi Merhi Balig Panossian Tamara Salloum Sima Tokajian SARS-CoV-2 and ORF3a: Nonsynonymous Mutations, Functional Domains, and Viral Pathogenesis
description	ABSTRACT The effect of the rapid accumulation of nonsynonymous mutations on the pathogenesis of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is not yet known. The 3a protein is unique to SARS-CoV and is essential for disease pathogenesis. Our study aimed at determining the nonsynonymous mutations in the 3a protein in SARS-CoV-2 and determining and characterizing the protein’s structure and spatial orientation in comparison to those of 3a in SARS-CoV. A total of 51 different nonsynonymous amino acid substitutions were detected in the 3a proteins among 2,782 SARS-CoV-2 strains. We observed microclonality within the ORF3a gene tree defined by nonsynonymous mutations separating the isolates into distinct subpopulations. We detected and identified six functional domains (I to VI) in the SARS-CoV-2 3a protein. The functional domains were linked to virulence, infectivity, ion channel formation, and virus release. Our study showed the importance of conserved functional domains across the species barrier and revealed the possible role of the 3a protein in the viral life cycle. Observations reported in this study merit experimental confirmation. IMPORTANCE At the surge of the coronavirus disease 2019 (COVID-19) pandemic, we detected and identified six functional domains (I to VI) in the SARS-CoV-2 3a protein. Our analysis showed that the functional domains were linked to virulence, infectivity, ion channel formation, and virus release in SARS-CoV-2 3a. Our study also revealed the functional importance of conserved domains across the species barrier. Observations reported in this study merit experimental confirmation.
format	article
author	Elio Issa Georgi Merhi Balig Panossian Tamara Salloum Sima Tokajian
author_facet	Elio Issa Georgi Merhi Balig Panossian Tamara Salloum Sima Tokajian
author_sort	Elio Issa
title	SARS-CoV-2 and ORF3a: Nonsynonymous Mutations, Functional Domains, and Viral Pathogenesis
title_short	SARS-CoV-2 and ORF3a: Nonsynonymous Mutations, Functional Domains, and Viral Pathogenesis
title_full	SARS-CoV-2 and ORF3a: Nonsynonymous Mutations, Functional Domains, and Viral Pathogenesis
title_fullStr	SARS-CoV-2 and ORF3a: Nonsynonymous Mutations, Functional Domains, and Viral Pathogenesis
title_full_unstemmed	SARS-CoV-2 and ORF3a: Nonsynonymous Mutations, Functional Domains, and Viral Pathogenesis
title_sort	sars-cov-2 and orf3a: nonsynonymous mutations, functional domains, and viral pathogenesis
publisher	American Society for Microbiology
publishDate	2020
url	https://doaj.org/article/17820af1c1a44c23afe10b4f64c46b29
work_keys_str_mv	AT elioissa sarscov2andorf3anonsynonymousmutationsfunctionaldomainsandviralpathogenesis AT georgimerhi sarscov2andorf3anonsynonymousmutationsfunctionaldomainsandviralpathogenesis AT baligpanossian sarscov2andorf3anonsynonymousmutationsfunctionaldomainsandviralpathogenesis AT tamarasalloum sarscov2andorf3anonsynonymousmutationsfunctionaldomainsandviralpathogenesis AT simatokajian sarscov2andorf3anonsynonymousmutationsfunctionaldomainsandviralpathogenesis
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SARS-CoV-2 and ORF3a: Nonsynonymous Mutations, Functional Domains, and Viral Pathogenesis

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