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

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SARS-CoV-2 is a betacoronavirus virus responsible for the COVID-19 pandemic. Here, we determined the X-ray crystal structure of a potent neutralizing monoclonal antibody, CV30, isolated from a patient infected with SARS-CoV-2, in complex with the receptor binding domain (RBD). The structure reveals...

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Autores principales: Hurlburt, Nicholas K., Wan, Yu-Hsin, Stuart, Andrew B., Feng, Junli, McGuire, Andrew T., Stamatatos, Leonidas, Pancera, Marie
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Cold Spring Harbor Laboratory 2020
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7301900/
https://www.ncbi.nlm.nih.gov/pubmed/32577631
http://dx.doi.org/10.1101/2020.06.12.148692
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author Hurlburt, Nicholas K.
Wan, Yu-Hsin
Stuart, Andrew B.
Feng, Junli
McGuire, Andrew T.
Stamatatos, Leonidas
Pancera, Marie
author_facet Hurlburt, Nicholas K.
Wan, Yu-Hsin
Stuart, Andrew B.
Feng, Junli
McGuire, Andrew T.
Stamatatos, Leonidas
Pancera, Marie
author_sort Hurlburt, Nicholas K.
collection PubMed
description SARS-CoV-2 is a betacoronavirus virus responsible for the COVID-19 pandemic. Here, we determined the X-ray crystal structure of a potent neutralizing monoclonal antibody, CV30, isolated from a patient infected with SARS-CoV-2, in complex with the receptor binding domain (RBD). The structure reveals CV30’s epitope overlaps with the human ACE2 receptor binding site thus providing the structural basis for its neutralization by preventing ACE2 binding.
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spelling pubmed-73019002020-06-23 Structural basis for potent neutralization of SARS-CoV-2 and role of antibody affinity maturation Hurlburt, Nicholas K. Wan, Yu-Hsin Stuart, Andrew B. Feng, Junli McGuire, Andrew T. Stamatatos, Leonidas Pancera, Marie bioRxiv Article SARS-CoV-2 is a betacoronavirus virus responsible for the COVID-19 pandemic. Here, we determined the X-ray crystal structure of a potent neutralizing monoclonal antibody, CV30, isolated from a patient infected with SARS-CoV-2, in complex with the receptor binding domain (RBD). The structure reveals CV30’s epitope overlaps with the human ACE2 receptor binding site thus providing the structural basis for its neutralization by preventing ACE2 binding. Cold Spring Harbor Laboratory 2020-06-12 /pmc/articles/PMC7301900/ /pubmed/32577631 http://dx.doi.org/10.1101/2020.06.12.148692 Text en https://creativecommons.org/licenses/by-nc-nd/4.0/It is made available under a CC-BY-NC-ND 4.0 International license (https://creativecommons.org/licenses/by-nc-nd/4.0/) .
spellingShingle Article
Hurlburt, Nicholas K.
Wan, Yu-Hsin
Stuart, Andrew B.
Feng, Junli
McGuire, Andrew T.
Stamatatos, Leonidas
Pancera, Marie
Structural basis for potent neutralization of SARS-CoV-2 and role of antibody affinity maturation
title 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_short 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
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7301900/
https://www.ncbi.nlm.nih.gov/pubmed/32577631
http://dx.doi.org/10.1101/2020.06.12.148692
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