Unexpected Receptor Functional Mimicry Elucidates Activation of Coronavirus Fusion

Walls, Alexandra C.; Xiong, Xiaoli; Park, Young-Jun; Tortorici, M. Alejandra; Snijder, Joost; Quispe, Joel; Cameroni, Elisabetta; Gopal, Robin; Dai, Mian; Lanzavecchia, Antonio; Zambon, Maria; Rey, Félix A.; Corti, Davide; Veesler, David

doi:10.1016/j.cell.2018.12.028

Cited by 586SARS-CoV-2 and COVID-19 ResearchAnimal Virus Infections Studiesvaccines and immunoinformatics approaches

Unexpected Receptor Functional Mimicry Elucidates Activation of Coronavirus Fusion

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Walls, Alexandra C., Xiong, Xiaoli, Park, Young-Jun, Tortorici, M. Alejandra, Snijder, Joost, Quispe, Joel, Cameroni, Elisabetta, Gopal, Robin +6 more·2019·Cell

DOI 10.1016/j.cell.2018.12.028PMC PMC6751136

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Abstract

Recent outbreaks of severe acute respiratory syndrome and Middle East respiratory syndrome, along with the threat of a future coronavirus-mediated pandemic, underscore the importance of finding ways to combat these viruses. The trimeric spike transmembrane glycoprotein S mediates entry into host cells and is the major target of neutralizing antibodies. To understand the humoral immune response elicited upon natural infections with coronaviruses, we structurally characterized the SARS-CoV and MERS-CoV S glycoproteins in complex with neutralizing antibodies isolated from human survivors. Although the two antibodies studied blocked attachment to the host cell receptor, only the anti-SARS-CoV S antibody triggered fusogenic conformational changes via receptor functional mimicry. These results provide a structural framework for understanding coronavirus neutralization by human antibodies and shed light on activation of coronavirus membrane fusion, which takes place through a receptor-driven ratcheting mechanism.

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Protection against SARS-CoV-2 is thought to be mediated by neutralizing antibodies against the S protein.
“Protection is thought to be mediated by neutralizing antibodies against the S protein (7, 8)”
From An Alphavirus -derived replicon RNA vaccine induces SARS-CoV-2 neutralizing antibody and T cell responses in mice and nonhuman primates (2020) · cites this paper as [7]
The Introduction (page not provided) calls the S glycoprotein the main target of neutralizing antibodies and describes antibodies from SARS-CoV and MERS-CoV survivors. The paper does not address SARS-CoV-2 or establish that these antibodies mediate protection against it. (LLM, conf=0.87)
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Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation
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Elicitation of Potent Neutralizing Antibody Responses by Designed Protein Nanoparticle Vaccines for SARS-CoV-2
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Structural basis for human coronavirus attachment to sialic acid receptors
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Broad neutralization of SARS-related viruses by human monoclonal antibodies
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SARS-CoV-2 RBD antibodies that maximize breadth and resistance to escape
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Drug targets for corona virus: A systematic review
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SARS-CoV-2 infects cells after viral entry via clathrin-mediated endocytosis
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Deducing the N- and O-glycosylation profile of the spike protein of novel coronavirus SARS-CoV-2
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Key residues of the receptor binding motif in the spike protein of SARS-CoV-2 that interact with ACE2 and neutralizing antibodies
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Seydoux, E., Homad, L. J., MacCamy, A. J., Parks, K. R., Hurlburt, N. K., Jennewein, M. F., Akins, N. R., Stuart, A. B., Wan, Y.-H., Feng, J., et al. (2020) · Immunity · doi:10.1016/j.immuni.2020.06.001 · Cited by 364 · see citing works
CoV-AbDab: the coronavirus antibody database
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Structural and functional characterizations of infectivity and immune evasion of SARS-CoV-2 Omicron
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Structural basis for neutralization of SARS-CoV-2 and SARS-CoV by a potent therapeutic antibody
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Vulnerabilities in coronavirus glycan shields despite extensive glycosylation
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Imprinted antibody responses against SARS-CoV-2 Omicron sublineages
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Structurally Resolved SARS-CoV-2 Antibody Shows High Efficacy in Severely Infected Hamsters and Provides a Potent Cocktail Pairing Strategy
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Authors: Walls, A. C., Xiong, X., Park, Y.-J., Tortorici, M. A., Snijder, J., Quispe, J., Cameroni, E., Gopal, R., Dai, M., Lanzavecchia, A., Zambon, M., Rey, F. A., Corti, D., & Veesler, D.
Affiliations: University of Washington (US)
Centre National de la Recherche Scientifique (FR)
Vir Biotechnology (Switzerland) (CH)
Public Health England (GB)
The Francis Crick Institute (GB)
Institute for Research in Biomedicine (CH)
Corresponding author: Veesler, David
ORCID: Walls, Alexandra C.
Xiong, Xiaoli
Park, Young-Jun
Tortorici, M. Alejandra
Snijder, Joost
Quispe, Joel
Cameroni, Elisabetta
Lanzavecchia, Antonio
Zambon, Maria
Corti, Davide
Veesler, David
Venue: Cell
Publisher: Elsevier BV
Published: 2019-02
Volume: 176
Issue: 5
Pages: 1026-1039.e15
ISSN: 0092-8674 (ISSN-L)
DOI: 10.1016/j.cell.2018.12.028
PMC: PMC6751136
OpenAlex: W2915009278
Cited by: 582
References: 85
Citations by year: 2026: 7 · 2025: 25 · 2024: 30 · 2023: 40 · 2022: 79 · 2021: 173 · 2020: 214 · 2019: 14
FWCI: 92.33
Type: journal article
Language: en
Update notices: erratum (2020-12-10)
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 385 d)
Locations: Cell (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
HAL (submittedVersion)
Utrecht University Repository (Utrecht University) (submittedVersion, other-oa)
Funders: National Institute of General Medical Sciences (R01GM120553)
National Institute of Allergy and Infectious Diseases (HHSN272201700059C)
Pew Biomedical Scholars Award
Burroughs Wellcome Fund
Netherlands Organisation for Scientific Research (Rubicon 019.2015.2.310.006)
European Molecular Biology Organization (ALTF933-2015)
Zoonoses Anticipation and Preparedness Initiative (IMI115760)
Pasteur Institute
Centre National de la Recherche Scientifique
LabEx Integrative Biology of Emerging Infectious Diseases
University of Washington Arnold and Mabel Beckman CryoEM Center and Proteomics Resource (UWPR95794)
Advanced Light Source at Lawrence Berkley National Laboratory
Topics: Health Sciences › Medicine › Infectious Diseases › SARS-CoV-2 and COVID-19 Research
Life Sciences › Agricultural and Biological Sciences › Animal Science and Zoology › Animal Virus Infections Studies
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › vaccines and immunoinformatics approaches
Keywords: SARS-CoV, MERS-CoV, neutralizing antibodies, antibody-antigen complex structure, humoral immune response, viral entry, receptor binding
MeSH terms: Animals, Antibodies, Monoclonal, Antibodies, Viral, Chlorocebus aethiops, Humans, Protein Binding, Receptors, Virus, Vero Cells, Coronavirus, Coronavirus Infections, Molecular Mimicry, Severe acute respiratory syndrome-related coronavirus, Virus Internalization, Immunity, Humoral, Antibodies, Neutralizing, HEK293 Cells, Spike Glycoprotein, Coronavirus, Middle East Respiratory Syndrome Coronavirus

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Unexpected Receptor Functional Mimicry Elucidates Activation of Coronavirus Fusion

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