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Structural basis for broad coronavirus neutralization
Preprint
in En
| PREPRINT-BIORXIV
| ID: ppbiorxiv-424482
Journal article
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A scientific journal published article is available and is probably based on this preprint. It has been identified through a machine matching algorithm, human confirmation is still pending.
See journal article
ABSTRACT
Three highly pathogenic {beta}-coronaviruses crossed the animal-to-human species barrier in the past two decades SARS-CoV, MERS-CoV and SARS-CoV-2. SARS-CoV-2 has infected more than 64 million people worldwide, claimed over 1.4 million lives and is responsible for the ongoing COVID-19 pandemic. We isolated a monoclonal antibody, termed B6, cross-reacting with eight {beta}-coronavirus spike glycoproteins, including all five human-infecting {beta}-coronaviruses, and broadly inhibiting entry of pseudotyped viruses from two coronavirus lineages. Cryo-electron microscopy and X-ray crystallography characterization reveal that B6 binds to a conserved cryptic epitope located in the fusion machinery and indicate that antibody binding sterically interferes with spike conformational changes leading to membrane fusion. Our data provide a structural framework explaining B6 cross-reactivity with {beta}-coronaviruses from three lineages along with proof-of-concept for antibody-mediated broad coronavirus neutralization elicited through vaccination. This study unveils an unexpected target for next-generation structure-guided design of a pan-coronavirus vaccine.
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Full text:
1
Collection:
09-preprints
Database:
PREPRINT-BIORXIV
Type of study:
Rct
Language:
En
Year:
2020
Document type:
Preprint