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Development and characterization of SARS-CoV-2 variant-neutralizing monoclonal antibodies
Vaccination and administration of monoclonal antibody cocktails are effective tools to control the progression of infectious diseases and to terminate pandemics such as COVID-19. However, the emergence of SARS-CoV-2 mutants with enhanced transmissibility and altered antigenicity requires broad-spect...
Autores principales: | , , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Published by Elsevier B.V.
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8572761/ https://www.ncbi.nlm.nih.gov/pubmed/34762975 http://dx.doi.org/10.1016/j.antiviral.2021.105206 |
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author | Qiu, Hongyu Yuan, Xin-Yong Cabral, Teresa Manguiat, Kathy Robinson, Alyssia Wood, Heidi Grant, Chris McQueen, Peter Westmacott, Garrett Beniac, Daniel R. Lin, Lisa Carpenter, Michael Kobasa, Darwyn Gräfenhan, Tom |
author_facet | Qiu, Hongyu Yuan, Xin-Yong Cabral, Teresa Manguiat, Kathy Robinson, Alyssia Wood, Heidi Grant, Chris McQueen, Peter Westmacott, Garrett Beniac, Daniel R. Lin, Lisa Carpenter, Michael Kobasa, Darwyn Gräfenhan, Tom |
author_sort | Qiu, Hongyu |
collection | PubMed |
description | Vaccination and administration of monoclonal antibody cocktails are effective tools to control the progression of infectious diseases and to terminate pandemics such as COVID-19. However, the emergence of SARS-CoV-2 mutants with enhanced transmissibility and altered antigenicity requires broad-spectrum therapies. Here we developed a panel of SARS-CoV-2 specific mouse monoclonal antibodies (mAbs), and characterized them based on ELISA, Western immunoblot, isotyping, and virus neutralization. Six neutralizing mAbs that exhibited high-affinity binding to SARS-CoV-2 spike protein were identified, and their amino acid sequences were determined by mass spectrometry. Functional assays confirmed that three mAbs, F461G11, F461G15, and F461G16 neutralized four variants of concern (VOC): B.1.1.7 (alpha), B.1.351 (beta), P.1 (gamma) and B.1.617.2 (delta) These mAbs are promising candidates for COVID-19 therapy, and understanding their interactions with virus spike protein should support further vaccine and antibody development. |
format | Online Article Text |
id | pubmed-8572761 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Published by Elsevier B.V. |
record_format | MEDLINE/PubMed |
spelling | pubmed-85727612021-11-08 Development and characterization of SARS-CoV-2 variant-neutralizing monoclonal antibodies Qiu, Hongyu Yuan, Xin-Yong Cabral, Teresa Manguiat, Kathy Robinson, Alyssia Wood, Heidi Grant, Chris McQueen, Peter Westmacott, Garrett Beniac, Daniel R. Lin, Lisa Carpenter, Michael Kobasa, Darwyn Gräfenhan, Tom Antiviral Res Article Vaccination and administration of monoclonal antibody cocktails are effective tools to control the progression of infectious diseases and to terminate pandemics such as COVID-19. However, the emergence of SARS-CoV-2 mutants with enhanced transmissibility and altered antigenicity requires broad-spectrum therapies. Here we developed a panel of SARS-CoV-2 specific mouse monoclonal antibodies (mAbs), and characterized them based on ELISA, Western immunoblot, isotyping, and virus neutralization. Six neutralizing mAbs that exhibited high-affinity binding to SARS-CoV-2 spike protein were identified, and their amino acid sequences were determined by mass spectrometry. Functional assays confirmed that three mAbs, F461G11, F461G15, and F461G16 neutralized four variants of concern (VOC): B.1.1.7 (alpha), B.1.351 (beta), P.1 (gamma) and B.1.617.2 (delta) These mAbs are promising candidates for COVID-19 therapy, and understanding their interactions with virus spike protein should support further vaccine and antibody development. Published by Elsevier B.V. 2021-12 2021-11-08 /pmc/articles/PMC8572761/ /pubmed/34762975 http://dx.doi.org/10.1016/j.antiviral.2021.105206 Text en © 2021 Published by Elsevier B.V. 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 Qiu, Hongyu Yuan, Xin-Yong Cabral, Teresa Manguiat, Kathy Robinson, Alyssia Wood, Heidi Grant, Chris McQueen, Peter Westmacott, Garrett Beniac, Daniel R. Lin, Lisa Carpenter, Michael Kobasa, Darwyn Gräfenhan, Tom Development and characterization of SARS-CoV-2 variant-neutralizing monoclonal antibodies |
title | Development and characterization of SARS-CoV-2 variant-neutralizing monoclonal antibodies |
title_full | Development and characterization of SARS-CoV-2 variant-neutralizing monoclonal antibodies |
title_fullStr | Development and characterization of SARS-CoV-2 variant-neutralizing monoclonal antibodies |
title_full_unstemmed | Development and characterization of SARS-CoV-2 variant-neutralizing monoclonal antibodies |
title_short | Development and characterization of SARS-CoV-2 variant-neutralizing monoclonal antibodies |
title_sort | development and characterization of sars-cov-2 variant-neutralizing monoclonal antibodies |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8572761/ https://www.ncbi.nlm.nih.gov/pubmed/34762975 http://dx.doi.org/10.1016/j.antiviral.2021.105206 |
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