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A review on evolution of emerging SARS-CoV-2 variants based on spike glycoprotein

Since the inception of SARS-CoV-2 in December 2019, many variants have emerged over time. Some of these variants have resulted in transmissibility changes of the virus and may also have impact on diagnosis, therapeutics and even vaccines, thereby raising particular concerns in the scientific communi...

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Autores principales: Ghosh, Nimisha, Nandi, Suman, Saha, Indrajit
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier B.V. 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8799522/
https://www.ncbi.nlm.nih.gov/pubmed/35123183
http://dx.doi.org/10.1016/j.intimp.2022.108565
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author Ghosh, Nimisha
Nandi, Suman
Saha, Indrajit
author_facet Ghosh, Nimisha
Nandi, Suman
Saha, Indrajit
author_sort Ghosh, Nimisha
collection PubMed
description Since the inception of SARS-CoV-2 in December 2019, many variants have emerged over time. Some of these variants have resulted in transmissibility changes of the virus and may also have impact on diagnosis, therapeutics and even vaccines, thereby raising particular concerns in the scientific community. The variants which have mutations in Spike glycoprotein are the primary focus as it is the main target for neutralising antibodies. SARS-CoV-2 is known to infect human through Spike glycoprotein and uses receptor-binding domain (RBD) to bind to the ACE2 receptor in human. Thus, it is of utmost importance to study these variants and their corresponding mutations. Such 12 different important variants identified so far are B.1.1.7 (Alpha), B.1.351 (Beta), B.1.525 (Eta), B.1.427/B.1.429 (Epsilon), B.1.526 (Iota), B.1.617.1 (Kappa), B.1.617.2 (Delta), C.37 (Lambda), P.1 (Gamma), P.2 (Zeta), P.3 (Theta) and the recently discovered B.1.1.529 (Omicron). These variants have 84 unique mutations in Spike glycoprotein. To analyse such mutations, multiple sequence alignment of 77681 SARS-CoV-2 genomes of 98 countries over the period from January 2020 to July 2021 is performed followed by phylogenetic analysis. Also, characteristics of new emerging variants are elaborately discussed. The individual evolution of these mutation points and the respective variants are visualised and their characteristics are also reported. Moreover, to judge the characteristics of the non-synonymous mutation points (substitutions), their biological functions are evaluated by PolyPhen-2 while protein structural stability is evaluated using I-Mutant 2.0.
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spelling pubmed-87995222022-01-31 A review on evolution of emerging SARS-CoV-2 variants based on spike glycoprotein Ghosh, Nimisha Nandi, Suman Saha, Indrajit Int Immunopharmacol Article Since the inception of SARS-CoV-2 in December 2019, many variants have emerged over time. Some of these variants have resulted in transmissibility changes of the virus and may also have impact on diagnosis, therapeutics and even vaccines, thereby raising particular concerns in the scientific community. The variants which have mutations in Spike glycoprotein are the primary focus as it is the main target for neutralising antibodies. SARS-CoV-2 is known to infect human through Spike glycoprotein and uses receptor-binding domain (RBD) to bind to the ACE2 receptor in human. Thus, it is of utmost importance to study these variants and their corresponding mutations. Such 12 different important variants identified so far are B.1.1.7 (Alpha), B.1.351 (Beta), B.1.525 (Eta), B.1.427/B.1.429 (Epsilon), B.1.526 (Iota), B.1.617.1 (Kappa), B.1.617.2 (Delta), C.37 (Lambda), P.1 (Gamma), P.2 (Zeta), P.3 (Theta) and the recently discovered B.1.1.529 (Omicron). These variants have 84 unique mutations in Spike glycoprotein. To analyse such mutations, multiple sequence alignment of 77681 SARS-CoV-2 genomes of 98 countries over the period from January 2020 to July 2021 is performed followed by phylogenetic analysis. Also, characteristics of new emerging variants are elaborately discussed. The individual evolution of these mutation points and the respective variants are visualised and their characteristics are also reported. Moreover, to judge the characteristics of the non-synonymous mutation points (substitutions), their biological functions are evaluated by PolyPhen-2 while protein structural stability is evaluated using I-Mutant 2.0. Elsevier B.V. 2022-04 2022-01-29 /pmc/articles/PMC8799522/ /pubmed/35123183 http://dx.doi.org/10.1016/j.intimp.2022.108565 Text en © 2022 Elsevier B.V. All rights reserved. Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active.
spellingShingle Article
Ghosh, Nimisha
Nandi, Suman
Saha, Indrajit
A review on evolution of emerging SARS-CoV-2 variants based on spike glycoprotein
title A review on evolution of emerging SARS-CoV-2 variants based on spike glycoprotein
title_full A review on evolution of emerging SARS-CoV-2 variants based on spike glycoprotein
title_fullStr A review on evolution of emerging SARS-CoV-2 variants based on spike glycoprotein
title_full_unstemmed A review on evolution of emerging SARS-CoV-2 variants based on spike glycoprotein
title_short A review on evolution of emerging SARS-CoV-2 variants based on spike glycoprotein
title_sort review on evolution of emerging sars-cov-2 variants based on spike glycoprotein
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8799522/
https://www.ncbi.nlm.nih.gov/pubmed/35123183
http://dx.doi.org/10.1016/j.intimp.2022.108565
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