Molecular strategies for antibody binding and escape of SARS-CoV-2 and its mutations

Abstract The COVID19 pandemic, caused by SARS-CoV-2, has infected more than 200 million people worldwide. Due to the rapid spreading of SARS-CoV-2 and its impact, it is paramount to find effective treatments against it. Human neutralizing antibodies are an effective method to fight viral infection....

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Autores principales:	Mohamed Hendy, Samuel Kaufman, Mauricio Ponga
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/801d7d3cdd074e7e8a37de7234682b42
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spelling	oai:doaj.org-article:801d7d3cdd074e7e8a37de7234682b422021-11-08T10:52:03ZMolecular strategies for antibody binding and escape of SARS-CoV-2 and its mutations10.1038/s41598-021-01081-02045-2322https://doaj.org/article/801d7d3cdd074e7e8a37de7234682b422021-11-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-01081-0https://doaj.org/toc/2045-2322Abstract The COVID19 pandemic, caused by SARS-CoV-2, has infected more than 200 million people worldwide. Due to the rapid spreading of SARS-CoV-2 and its impact, it is paramount to find effective treatments against it. Human neutralizing antibodies are an effective method to fight viral infection. However, the recent discovery of new strains that substantially change the S-protein sequence has raised concern about vaccines and antibodies’ effectiveness. Here, using molecular simulations, we investigated the binding mechanisms between the S-protein and several antibodies. Multiple mutations were included to understand the strategies for antibody escape in new variants. We found that the combination of mutations K417N, E484K, L452R, and T478K produced higher binding energy to ACE2 than the wild type, suggesting higher efficiency to enter host cells. The mutations’ effect depends on the antibody class. While Class I enhances the binding avidity in the presence of N501Y mutation, class II antibodies showed a sharp decline in the binding affinity. Our simulations suggest that Class I antibodies will remain effective against the new strains. In contrast, Class II antibodies will have less affinity to the S-protein, potentially affecting these antibodies’ efficiency.Mohamed HendySamuel KaufmanMauricio PongaNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-11 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Mohamed Hendy Samuel Kaufman Mauricio Ponga Molecular strategies for antibody binding and escape of SARS-CoV-2 and its mutations
description	Abstract The COVID19 pandemic, caused by SARS-CoV-2, has infected more than 200 million people worldwide. Due to the rapid spreading of SARS-CoV-2 and its impact, it is paramount to find effective treatments against it. Human neutralizing antibodies are an effective method to fight viral infection. However, the recent discovery of new strains that substantially change the S-protein sequence has raised concern about vaccines and antibodies’ effectiveness. Here, using molecular simulations, we investigated the binding mechanisms between the S-protein and several antibodies. Multiple mutations were included to understand the strategies for antibody escape in new variants. We found that the combination of mutations K417N, E484K, L452R, and T478K produced higher binding energy to ACE2 than the wild type, suggesting higher efficiency to enter host cells. The mutations’ effect depends on the antibody class. While Class I enhances the binding avidity in the presence of N501Y mutation, class II antibodies showed a sharp decline in the binding affinity. Our simulations suggest that Class I antibodies will remain effective against the new strains. In contrast, Class II antibodies will have less affinity to the S-protein, potentially affecting these antibodies’ efficiency.
format	article
author	Mohamed Hendy Samuel Kaufman Mauricio Ponga
author_facet	Mohamed Hendy Samuel Kaufman Mauricio Ponga
author_sort	Mohamed Hendy
title	Molecular strategies for antibody binding and escape of SARS-CoV-2 and its mutations
title_short	Molecular strategies for antibody binding and escape of SARS-CoV-2 and its mutations
title_full	Molecular strategies for antibody binding and escape of SARS-CoV-2 and its mutations
title_fullStr	Molecular strategies for antibody binding and escape of SARS-CoV-2 and its mutations
title_full_unstemmed	Molecular strategies for antibody binding and escape of SARS-CoV-2 and its mutations
title_sort	molecular strategies for antibody binding and escape of sars-cov-2 and its mutations
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/801d7d3cdd074e7e8a37de7234682b42
work_keys_str_mv	AT mohamedhendy molecularstrategiesforantibodybindingandescapeofsarscov2anditsmutations AT samuelkaufman molecularstrategiesforantibodybindingandescapeofsarscov2anditsmutations AT mauricioponga molecularstrategiesforantibodybindingandescapeofsarscov2anditsmutations
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Molecular strategies for antibody binding and escape of SARS-CoV-2 and its mutations

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