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Omicron variant and change of electrostatic interactions between receptor binding domain of severe acute respiratory syndrome coronavirus 2 with the angiotensin-converting enzyme 2 receptor

BACKGROUND: Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) variants are currently a new hazard. Since the first appearance of classical SARS-CoV-2 in late 2019, pathogen genetic alterations have continued to occur, and some new hazardous forms have already emerged. The underlying patho...

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Autores principales: Mungmunpuntipantip, Rujittika, Wiwanitkit, Viroj
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Baishideng Publishing Group Inc 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9150028/
https://www.ncbi.nlm.nih.gov/pubmed/35665239
http://dx.doi.org/10.5501/wjv.v11.i3.144
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author Mungmunpuntipantip, Rujittika
Wiwanitkit, Viroj
author_facet Mungmunpuntipantip, Rujittika
Wiwanitkit, Viroj
author_sort Mungmunpuntipantip, Rujittika
collection PubMed
description BACKGROUND: Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) variants are currently a new hazard. Since the first appearance of classical SARS-CoV-2 in late 2019, pathogen genetic alterations have continued to occur, and some new hazardous forms have already emerged. The underlying pathophysiological process leading to clinical issue is molecular change caused by genetic mutation. AIM: To determine the change in the interaction between receptor binding domain of omicron variant SARS-CoV-2 and the angiotensin-converting enzyme 2 (ACE2). METHODS: The researchers investigated how alterations in the binding area of the SARS receptor CoV2 interacted electrostatically with the ACE2 receptor. In this report, three important coronavirus disease 2019 variants, beta, delta, and omicron, were investigated. RESULTS: According to this study, there was a change of electrostatic interactions between the receptor binding domain of SARS-CoV-2 with the ACE2 receptor due to each studied variant. The most change was detected in omicron variant followed by delta variant and beta variant. CONCLUSION: Our results may support the clinical finding that the omicron variant is more transmissible than the wild type and other variants.
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spelling pubmed-91500282022-06-04 Omicron variant and change of electrostatic interactions between receptor binding domain of severe acute respiratory syndrome coronavirus 2 with the angiotensin-converting enzyme 2 receptor Mungmunpuntipantip, Rujittika Wiwanitkit, Viroj World J Virol Basic Study BACKGROUND: Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) variants are currently a new hazard. Since the first appearance of classical SARS-CoV-2 in late 2019, pathogen genetic alterations have continued to occur, and some new hazardous forms have already emerged. The underlying pathophysiological process leading to clinical issue is molecular change caused by genetic mutation. AIM: To determine the change in the interaction between receptor binding domain of omicron variant SARS-CoV-2 and the angiotensin-converting enzyme 2 (ACE2). METHODS: The researchers investigated how alterations in the binding area of the SARS receptor CoV2 interacted electrostatically with the ACE2 receptor. In this report, three important coronavirus disease 2019 variants, beta, delta, and omicron, were investigated. RESULTS: According to this study, there was a change of electrostatic interactions between the receptor binding domain of SARS-CoV-2 with the ACE2 receptor due to each studied variant. The most change was detected in omicron variant followed by delta variant and beta variant. CONCLUSION: Our results may support the clinical finding that the omicron variant is more transmissible than the wild type and other variants. Baishideng Publishing Group Inc 2022-05-25 2022-05-25 /pmc/articles/PMC9150028/ /pubmed/35665239 http://dx.doi.org/10.5501/wjv.v11.i3.144 Text en ©The Author(s) 2022. Published by Baishideng Publishing Group Inc. All rights reserved. https://creativecommons.org/licenses/by-nc/4.0/This article is an open-access article that was selected by an in-house editor and fully peer-reviewed by external reviewers. It is distributed in accordance with the Creative Commons Attribution NonCommercial (CC BY-NC 4.0) license, which permits others to distribute, remix, adapt, build upon this work non-commercially, and license their derivative works on different terms, provided the original work is properly cited and the use is non-commercial.
spellingShingle Basic Study
Mungmunpuntipantip, Rujittika
Wiwanitkit, Viroj
Omicron variant and change of electrostatic interactions between receptor binding domain of severe acute respiratory syndrome coronavirus 2 with the angiotensin-converting enzyme 2 receptor
title Omicron variant and change of electrostatic interactions between receptor binding domain of severe acute respiratory syndrome coronavirus 2 with the angiotensin-converting enzyme 2 receptor
title_full Omicron variant and change of electrostatic interactions between receptor binding domain of severe acute respiratory syndrome coronavirus 2 with the angiotensin-converting enzyme 2 receptor
title_fullStr Omicron variant and change of electrostatic interactions between receptor binding domain of severe acute respiratory syndrome coronavirus 2 with the angiotensin-converting enzyme 2 receptor
title_full_unstemmed Omicron variant and change of electrostatic interactions between receptor binding domain of severe acute respiratory syndrome coronavirus 2 with the angiotensin-converting enzyme 2 receptor
title_short Omicron variant and change of electrostatic interactions between receptor binding domain of severe acute respiratory syndrome coronavirus 2 with the angiotensin-converting enzyme 2 receptor
title_sort omicron variant and change of electrostatic interactions between receptor binding domain of severe acute respiratory syndrome coronavirus 2 with the angiotensin-converting enzyme 2 receptor
topic Basic Study
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9150028/
https://www.ncbi.nlm.nih.gov/pubmed/35665239
http://dx.doi.org/10.5501/wjv.v11.i3.144
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