Structural basis for potent neutralization of SARS-CoV-2 and role of antibody affinity maturation

Currently there is neither a vaccine nor an effective treatment strategy available for COVID19. Here, Hurlburt et al. provide the crystal structure of a patient-derived monoclonal antibody neutralizing SARS-CoV-2 via shedding of the S1 subunit and competing for the receptor binding domain.

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Autores principales:	Nicholas K. Hurlburt, Emilie Seydoux, Yu-Hsin Wan, Venkata Viswanadh Edara, Andrew B. Stuart, Junli Feng, Mehul S. Suthar, Andrew T. McGuire, Leonidas Stamatatos, Marie Pancera
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/db69f59e4cb349f0a8827bbe7916aae3
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spelling	oai:doaj.org-article:db69f59e4cb349f0a8827bbe7916aae32021-12-02T14:41:25ZStructural basis for potent neutralization of SARS-CoV-2 and role of antibody affinity maturation10.1038/s41467-020-19231-92041-1723https://doaj.org/article/db69f59e4cb349f0a8827bbe7916aae32020-10-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-19231-9https://doaj.org/toc/2041-1723Currently there is neither a vaccine nor an effective treatment strategy available for COVID19. Here, Hurlburt et al. provide the crystal structure of a patient-derived monoclonal antibody neutralizing SARS-CoV-2 via shedding of the S1 subunit and competing for the receptor binding domain.Nicholas K. HurlburtEmilie SeydouxYu-Hsin WanVenkata Viswanadh EdaraAndrew B. StuartJunli FengMehul S. SutharAndrew T. McGuireLeonidas StamatatosMarie PanceraNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-7 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Nicholas K. Hurlburt Emilie Seydoux Yu-Hsin Wan Venkata Viswanadh Edara Andrew B. Stuart Junli Feng Mehul S. Suthar Andrew T. McGuire Leonidas Stamatatos Marie Pancera Structural basis for potent neutralization of SARS-CoV-2 and role of antibody affinity maturation
description	Currently there is neither a vaccine nor an effective treatment strategy available for COVID19. Here, Hurlburt et al. provide the crystal structure of a patient-derived monoclonal antibody neutralizing SARS-CoV-2 via shedding of the S1 subunit and competing for the receptor binding domain.
format	article
author	Nicholas K. Hurlburt Emilie Seydoux Yu-Hsin Wan Venkata Viswanadh Edara Andrew B. Stuart Junli Feng Mehul S. Suthar Andrew T. McGuire Leonidas Stamatatos Marie Pancera
author_facet	Nicholas K. Hurlburt Emilie Seydoux Yu-Hsin Wan Venkata Viswanadh Edara Andrew B. Stuart Junli Feng Mehul S. Suthar Andrew T. McGuire Leonidas Stamatatos Marie Pancera
author_sort	Nicholas K. Hurlburt
title	Structural basis for potent neutralization of SARS-CoV-2 and role of antibody affinity maturation
title_short	Structural basis for potent neutralization of SARS-CoV-2 and role of antibody affinity maturation
title_full	Structural basis for potent neutralization of SARS-CoV-2 and role of antibody affinity maturation
title_fullStr	Structural basis for potent neutralization of SARS-CoV-2 and role of antibody affinity maturation
title_full_unstemmed	Structural basis for potent neutralization of SARS-CoV-2 and role of antibody affinity maturation
title_sort	structural basis for potent neutralization of sars-cov-2 and role of antibody affinity maturation
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/db69f59e4cb349f0a8827bbe7916aae3
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Structural basis for potent neutralization of SARS-CoV-2 and role of antibody affinity maturation

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