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In Vitro and In Vivo Characterization of a Broadly Neutralizing Anti-SARS-CoV-2 Antibody Isolated from a Semi-Immune Phage Display Library
Neutralizing antibodies targeting the receptor-binding domain (RBD) of SARS-CoV-2 are among the most promising strategies to prevent and/or treat COVID-19. However, as SARS-CoV-2 has evolved into new variants, most of the neutralizing antibodies authorized by the US FDA and/or EMA to treat COVID-19...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9496002/ https://www.ncbi.nlm.nih.gov/pubmed/36134953 http://dx.doi.org/10.3390/antib11030057 |
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author | González-González, Edith Carballo-Uicab, Gregorio Salinas-Trujano, Juana Cortés-Paniagua, María I. Vázquez-Leyva, Said Vallejo-Castillo, Luis Mendoza-Salazar, Ivette Gómez-Castellano, Keyla Pérez-Tapia, Sonia M. Almagro, Juan C. |
author_facet | González-González, Edith Carballo-Uicab, Gregorio Salinas-Trujano, Juana Cortés-Paniagua, María I. Vázquez-Leyva, Said Vallejo-Castillo, Luis Mendoza-Salazar, Ivette Gómez-Castellano, Keyla Pérez-Tapia, Sonia M. Almagro, Juan C. |
author_sort | González-González, Edith |
collection | PubMed |
description | Neutralizing antibodies targeting the receptor-binding domain (RBD) of SARS-CoV-2 are among the most promising strategies to prevent and/or treat COVID-19. However, as SARS-CoV-2 has evolved into new variants, most of the neutralizing antibodies authorized by the US FDA and/or EMA to treat COVID-19 have shown reduced efficacy or have failed to neutralize the variants of concern (VOCs), particularly B.1.1.529 (Omicron). Previously, we reported the discovery and characterization of antibodies with high affinity for SARS-CoV-2 RBD Wuhan (WT), B.1.617.2 (Delta), and B.1.1.529 (Omicron) strains. One of the antibodies, called IgG-A7, also blocked the interaction of human angiotensin-converting enzyme 2 (hACE2) with the RBDs of the three strains, suggesting it may be a broadly SARS-CoV-2 neutralizing antibody. Herein, we show that IgG-A7 efficiently neutralizes all the three SARS-CoV-2 strains in plaque reduction neutralization tests (PRNTs). In addition, we demonstrate that IgG-A7 fully protects K18-hACE2 transgenic mice infected with SARS-CoV-2 WT. Taken together, our findings indicate that IgG-A7 could be a suitable candidate for development of antibody-based drugs to treat and/or prevent SARS-CoV-2 VOCs infection. |
format | Online Article Text |
id | pubmed-9496002 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-94960022022-09-23 In Vitro and In Vivo Characterization of a Broadly Neutralizing Anti-SARS-CoV-2 Antibody Isolated from a Semi-Immune Phage Display Library González-González, Edith Carballo-Uicab, Gregorio Salinas-Trujano, Juana Cortés-Paniagua, María I. Vázquez-Leyva, Said Vallejo-Castillo, Luis Mendoza-Salazar, Ivette Gómez-Castellano, Keyla Pérez-Tapia, Sonia M. Almagro, Juan C. Antibodies (Basel) Article Neutralizing antibodies targeting the receptor-binding domain (RBD) of SARS-CoV-2 are among the most promising strategies to prevent and/or treat COVID-19. However, as SARS-CoV-2 has evolved into new variants, most of the neutralizing antibodies authorized by the US FDA and/or EMA to treat COVID-19 have shown reduced efficacy or have failed to neutralize the variants of concern (VOCs), particularly B.1.1.529 (Omicron). Previously, we reported the discovery and characterization of antibodies with high affinity for SARS-CoV-2 RBD Wuhan (WT), B.1.617.2 (Delta), and B.1.1.529 (Omicron) strains. One of the antibodies, called IgG-A7, also blocked the interaction of human angiotensin-converting enzyme 2 (hACE2) with the RBDs of the three strains, suggesting it may be a broadly SARS-CoV-2 neutralizing antibody. Herein, we show that IgG-A7 efficiently neutralizes all the three SARS-CoV-2 strains in plaque reduction neutralization tests (PRNTs). In addition, we demonstrate that IgG-A7 fully protects K18-hACE2 transgenic mice infected with SARS-CoV-2 WT. Taken together, our findings indicate that IgG-A7 could be a suitable candidate for development of antibody-based drugs to treat and/or prevent SARS-CoV-2 VOCs infection. MDPI 2022-09-06 /pmc/articles/PMC9496002/ /pubmed/36134953 http://dx.doi.org/10.3390/antib11030057 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article González-González, Edith Carballo-Uicab, Gregorio Salinas-Trujano, Juana Cortés-Paniagua, María I. Vázquez-Leyva, Said Vallejo-Castillo, Luis Mendoza-Salazar, Ivette Gómez-Castellano, Keyla Pérez-Tapia, Sonia M. Almagro, Juan C. In Vitro and In Vivo Characterization of a Broadly Neutralizing Anti-SARS-CoV-2 Antibody Isolated from a Semi-Immune Phage Display Library |
title | In Vitro and In Vivo Characterization of a Broadly Neutralizing Anti-SARS-CoV-2 Antibody Isolated from a Semi-Immune Phage Display Library |
title_full | In Vitro and In Vivo Characterization of a Broadly Neutralizing Anti-SARS-CoV-2 Antibody Isolated from a Semi-Immune Phage Display Library |
title_fullStr | In Vitro and In Vivo Characterization of a Broadly Neutralizing Anti-SARS-CoV-2 Antibody Isolated from a Semi-Immune Phage Display Library |
title_full_unstemmed | In Vitro and In Vivo Characterization of a Broadly Neutralizing Anti-SARS-CoV-2 Antibody Isolated from a Semi-Immune Phage Display Library |
title_short | In Vitro and In Vivo Characterization of a Broadly Neutralizing Anti-SARS-CoV-2 Antibody Isolated from a Semi-Immune Phage Display Library |
title_sort | in vitro and in vivo characterization of a broadly neutralizing anti-sars-cov-2 antibody isolated from a semi-immune phage display library |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9496002/ https://www.ncbi.nlm.nih.gov/pubmed/36134953 http://dx.doi.org/10.3390/antib11030057 |
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