A combination of cross-neutralizing antibodies synergizes to prevent SARS-CoV-2 and SARS-CoV pseudovirus infection
Autor: | Linghang Peng, Fangzhu Zhao, Meng Yuan, Xueyong Zhu, Dennis R. Burton, Hejun Liu, Nicholas C. Wu, Chang-Chun D Lee, Marit J. van Gils, David Nemazee, Deli Huang, Sandhya Bangaru, Ian A. Wilson, Hans Christian Kornau, Shawn Barman, Harald Prüss, Rogier W. Sanders, Jakob Kreye, S. Momsen Reincke, Andrew B. Ward |
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Přispěvatelé: | Medical Microbiology and Infection Prevention, AII - Infectious diseases |
Rok vydání: | 2021 |
Předmět: |
viruses
cross-neutralizing antibody coronavirus synergy 3D structure Antibodies Viral Severe Acute Respiratory Syndrome medicine.disease_cause metabolism [Angiotensin-Converting Enzyme 2] chemistry [Antibodies Viral] immunology [SARS Virus] Neutralization 0302 clinical medicine Pandemic immunology [SARS-CoV-2] prevention & control [Severe Acute Respiratory Syndrome] skin and connective tissue diseases Coronavirus 0303 health sciences biology virus diseases immunology [Severe acute respiratory syndrome-related coronavirus] Severe acute respiratory syndrome-related coronavirus Spike Glycoprotein Coronavirus Angiotensin-Converting Enzyme 2 Antibody 2019-20 coronavirus outbreak Coronavirus disease 2019 (COVID-19) Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) ACE2 protein human prevention & control [COVID-19] Cross Reactions Microbiology Article Antigenic drift immunology [Antibodies Viral] antibody cocktail chemistry [Antibodies Neutralizing] 03 medical and health sciences ddc:570 Virology medicine Antigenic variation Humans crystallography 030304 developmental biology SARS-CoV-2 fungi COVID-19 Antibodies Neutralizing immunology [Antibodies Neutralizing] body regions metabolism [Spike Glycoprotein Coronavirus] antibody-antigen interaction biology.protein Parasitology 030217 neurology & neurosurgery |
Zdroj: | bioRxiv article-version (status) pre article-version (number) 1 Cell host & microbe, 29(5), 806-818.e6. Cell Press Cell host and microbe 29(5), 806-818.e6 (2021). doi:10.1016/j.chom.2021.04.005 Cell Host & Microbe |
ISSN: | 1931-3128 |
DOI: | 10.1016/j.chom.2021.04.005 |
Popis: | Coronaviruses have caused several human epidemics and pandemics including the ongoing coronavirus disease 2019 (COVID-19). Prophylactic vaccines and therapeutic antibodies have already shown striking effectiveness against COVID-19. Nevertheless, concerns remain about antigenic drift in SARS-CoV-2 as well as threats from other sarbecoviruses. Cross-neutralizing antibodies to SARS-related viruses provide opportunities to address such concerns. Here, we report on crystal structures of a cross-neutralizing antibody, CV38-142, in complex with the receptor-binding domains from SARS-CoV-2 and SARS-CoV. Recognition of the N343 glycosylation site and water-mediated interactions facilitate cross-reactivity of CV38-142 to SARS-related viruses, allowing the antibody to accommodate antigenic variation in these viruses. CV38-142 synergizes with other cross-neutralizing antibodies, notably COVA1-16, to enhance neutralization of SARS-CoV and SARS-CoV-2, including circulating variants of concern B.1.1.7 and B.1.351. Overall, this study provides valuable information for vaccine and therapeutic design to address current and future antigenic drift in SARS-CoV-2 and to protect against zoonotic SARS-related coronaviruses. Graphical abstract Antibody CV38-142 from a COVID-19 patient cross-reacts with SARS-related viruses. Liu et al. reveal that CV38-142 interacts with the S309 N343 glycan site and synergizes with COVA1-16 that binds the conserved CR3022 site. Combination of the two cross-neutralizing antibodies shows enhanced neutralization to circulating variants of concern B.1.1.7 and B.1.351. |
Databáze: | OpenAIRE |
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