Journal
CELL
Volume 176, Issue 5, Pages 1026-+Publisher
CELL PRESS
DOI: 10.1016/j.cell.2018.12.028
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Funding
- 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]
- beamline 5.0.1 at the Advanced Light Source at Lawrence Berkley National Laboratory
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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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