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Omicron SARS-CoV-2 variant: Unique features and their impact on pre-existing antibodies
Severe Acute Respiratory Coronavirus (SARS-CoV-2) has been emerging in the form of different variants since its first emergence in early December 2019. A new Variant of Concern (VOC) named the Omicron variant (B.1.1.529) was reported recently. This variant has a large number of mutations in the S pr...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Elsevier Ltd.
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8666303/ https://www.ncbi.nlm.nih.gov/pubmed/34915422 http://dx.doi.org/10.1016/j.jaut.2021.102779 |
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author | Kannan, Saathvik R. Spratt, Austin N. Sharma, Kalicharan Chand, Hitendra S. Byrareddy, Siddappa N. Singh, Kamal |
author_facet | Kannan, Saathvik R. Spratt, Austin N. Sharma, Kalicharan Chand, Hitendra S. Byrareddy, Siddappa N. Singh, Kamal |
author_sort | Kannan, Saathvik R. |
collection | PubMed |
description | Severe Acute Respiratory Coronavirus (SARS-CoV-2) has been emerging in the form of different variants since its first emergence in early December 2019. A new Variant of Concern (VOC) named the Omicron variant (B.1.1.529) was reported recently. This variant has a large number of mutations in the S protein. To date, there exists a limited information on the Omicron variant. Here we present the analyses of mutation distribution, the evolutionary relationship of Omicron with previous variants, and probable structural impact of mutations on antibody binding. Our analyses show the presence of 46 high prevalence mutations specific to Omicron. Twenty-three of these are localized within the spike (S) protein and the rest localized to the other 3 structural proteins of the virus, the envelope (E), membrane (M), and nucleocapsid (N). Phylogenetic analysis showed that the Omicron is closely related to the Gamma (P.1) variant. The structural analyses showed that several mutations are localized to the region of the S protein that is the major target of antibodies, suggesting that the mutations in the Omicron variant may affect the binding affinities of antibodies to the S protein. |
format | Online Article Text |
id | pubmed-8666303 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Elsevier Ltd. |
record_format | MEDLINE/PubMed |
spelling | pubmed-86663032021-12-14 Omicron SARS-CoV-2 variant: Unique features and their impact on pre-existing antibodies Kannan, Saathvik R. Spratt, Austin N. Sharma, Kalicharan Chand, Hitendra S. Byrareddy, Siddappa N. Singh, Kamal J Autoimmun Article Severe Acute Respiratory Coronavirus (SARS-CoV-2) has been emerging in the form of different variants since its first emergence in early December 2019. A new Variant of Concern (VOC) named the Omicron variant (B.1.1.529) was reported recently. This variant has a large number of mutations in the S protein. To date, there exists a limited information on the Omicron variant. Here we present the analyses of mutation distribution, the evolutionary relationship of Omicron with previous variants, and probable structural impact of mutations on antibody binding. Our analyses show the presence of 46 high prevalence mutations specific to Omicron. Twenty-three of these are localized within the spike (S) protein and the rest localized to the other 3 structural proteins of the virus, the envelope (E), membrane (M), and nucleocapsid (N). Phylogenetic analysis showed that the Omicron is closely related to the Gamma (P.1) variant. The structural analyses showed that several mutations are localized to the region of the S protein that is the major target of antibodies, suggesting that the mutations in the Omicron variant may affect the binding affinities of antibodies to the S protein. Elsevier Ltd. 2022-01 2021-12-13 /pmc/articles/PMC8666303/ /pubmed/34915422 http://dx.doi.org/10.1016/j.jaut.2021.102779 Text en © 2021 Elsevier Ltd. 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 Kannan, Saathvik R. Spratt, Austin N. Sharma, Kalicharan Chand, Hitendra S. Byrareddy, Siddappa N. Singh, Kamal Omicron SARS-CoV-2 variant: Unique features and their impact on pre-existing antibodies |
title | Omicron SARS-CoV-2 variant: Unique features and their impact on pre-existing antibodies |
title_full | Omicron SARS-CoV-2 variant: Unique features and their impact on pre-existing antibodies |
title_fullStr | Omicron SARS-CoV-2 variant: Unique features and their impact on pre-existing antibodies |
title_full_unstemmed | Omicron SARS-CoV-2 variant: Unique features and their impact on pre-existing antibodies |
title_short | Omicron SARS-CoV-2 variant: Unique features and their impact on pre-existing antibodies |
title_sort | omicron sars-cov-2 variant: unique features and their impact on pre-existing antibodies |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8666303/ https://www.ncbi.nlm.nih.gov/pubmed/34915422 http://dx.doi.org/10.1016/j.jaut.2021.102779 |
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