Structural basis for broad coronavirus neutralization View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2021-05-12

AUTHORS

Maximilian M. Sauer, M. Alejandra Tortorici, Young-Jun Park, Alexandra C. Walls, Leah Homad, Oliver J. Acton, John E. Bowen, Chunyan Wang, Xiaoli Xiong, Willem de van der Schueren, Joel Quispe, Benjamin G. Hoffstrom, Berend-Jan Bosch, Andrew T. McGuire, David Veesler

ABSTRACT

Three highly pathogenic β-coronaviruses have crossed the animal-to-human species barrier in the past two decades: SARS-CoV, MERS-CoV and SARS-CoV-2. To evaluate the possibility of identifying antibodies with broad neutralizing activity, we isolated a monoclonal antibody, termed B6, that cross-reacts with eight β-coronavirus spike glycoproteins, including all five human-infecting β-coronaviruses. B6 broadly neutralizes entry of pseudotyped viruses from lineages A and C, but not from lineage B, and the latter includes SARS-CoV and SARS-CoV-2. Cryo-EM, X-ray crystallography and membrane fusion assays reveal that B6 binds to a conserved cryptic epitope located in the fusion machinery. The data indicate that antibody binding sterically interferes with the spike conformational changes leading to membrane fusion. Our data provide a structural framework explaining B6 cross-reactivity with β-coronaviruses from three lineages, along with a 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-β-coronavirus vaccine. More... »

PAGES

478-486

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/s41594-021-00596-4

    DOI

    http://dx.doi.org/10.1038/s41594-021-00596-4

    DIMENSIONS

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    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/33981021


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