Antibody-mediated disruption of the SARS-CoV-2 spike glycoprotein

The CR3022 antibody, selected from a group of SARS-CoV monoclonal antibodies for its ability to cross-react with SARS-CoV-2, has been examined for its ability to bind to the ectodomain of the SARS-CoV-2 spike glycoprotein. Using cryo-electron microscopy we show that antibody binding requires rearran...

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Autores principales: Wrobel, Antoni G., Benton, Donald J., Hussain, Saira, Harvey, Ruth, Martin, Stephen R., Roustan, Chloë, Rosenthal, Peter B., Skehel, John J., Gamblin, Steven J.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2020
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7577971/
https://www.ncbi.nlm.nih.gov/pubmed/33087721
http://dx.doi.org/10.1038/s41467-020-19146-5
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author Wrobel, Antoni G.
Benton, Donald J.
Hussain, Saira
Harvey, Ruth
Martin, Stephen R.
Roustan, Chloë
Rosenthal, Peter B.
Skehel, John J.
Gamblin, Steven J.
author_facet Wrobel, Antoni G.
Benton, Donald J.
Hussain, Saira
Harvey, Ruth
Martin, Stephen R.
Roustan, Chloë
Rosenthal, Peter B.
Skehel, John J.
Gamblin, Steven J.
author_sort Wrobel, Antoni G.
collection PubMed
description The CR3022 antibody, selected from a group of SARS-CoV monoclonal antibodies for its ability to cross-react with SARS-CoV-2, has been examined for its ability to bind to the ectodomain of the SARS-CoV-2 spike glycoprotein. Using cryo-electron microscopy we show that antibody binding requires rearrangements in the S1 domain that result in dissociation of the spike.
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spelling pubmed-75779712020-10-29 Antibody-mediated disruption of the SARS-CoV-2 spike glycoprotein Wrobel, Antoni G. Benton, Donald J. Hussain, Saira Harvey, Ruth Martin, Stephen R. Roustan, Chloë Rosenthal, Peter B. Skehel, John J. Gamblin, Steven J. Nat Commun Article The CR3022 antibody, selected from a group of SARS-CoV monoclonal antibodies for its ability to cross-react with SARS-CoV-2, has been examined for its ability to bind to the ectodomain of the SARS-CoV-2 spike glycoprotein. Using cryo-electron microscopy we show that antibody binding requires rearrangements in the S1 domain that result in dissociation of the spike. Nature Publishing Group UK 2020-10-21 /pmc/articles/PMC7577971/ /pubmed/33087721 http://dx.doi.org/10.1038/s41467-020-19146-5 Text en © The Author(s) 2020 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Article
Wrobel, Antoni G.
Benton, Donald J.
Hussain, Saira
Harvey, Ruth
Martin, Stephen R.
Roustan, Chloë
Rosenthal, Peter B.
Skehel, John J.
Gamblin, Steven J.
Antibody-mediated disruption of the SARS-CoV-2 spike glycoprotein
title Antibody-mediated disruption of the SARS-CoV-2 spike glycoprotein
title_full Antibody-mediated disruption of the SARS-CoV-2 spike glycoprotein
title_fullStr Antibody-mediated disruption of the SARS-CoV-2 spike glycoprotein
title_full_unstemmed Antibody-mediated disruption of the SARS-CoV-2 spike glycoprotein
title_short Antibody-mediated disruption of the SARS-CoV-2 spike glycoprotein
title_sort antibody-mediated disruption of the sars-cov-2 spike glycoprotein
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7577971/
https://www.ncbi.nlm.nih.gov/pubmed/33087721
http://dx.doi.org/10.1038/s41467-020-19146-5
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