Evidence map›Paper›PMID 33398277›Full record

ArticlebioRxiv : the preprint server for biology2021

Structural basis for broad coronavirus neutralization.

Maximilian M Sauer, M Alexandra Tortorici, Young-Jun Park, Alexandra C Walls, Leah Homad, Oliver Acton, John Bowen, Chunyan Wang, Xiaoli Xiong, Willem de van der Schueren and 5 more

Open access · greenAbstract readPreprint
PubMed Full text at PMC Publisher
In one paragraph

Article in bioRxiv : the preprint server for biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed, 43 citations in OpenAlex.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

15 authors at 4 institutions in 3 countries.

Maximilian M SauerDepartment of Biochemistry, University of Washington, Seattle, Washington 98195, USA.
M Alexandra TortoriciDepartment of Biochemistry, University of Washington, Seattle, Washington 98195, USA.
Young-Jun ParkDepartment of Biochemistry, University of Washington, Seattle, Washington 98195, USA.
Alexandra C WallsDepartment of Biochemistry, University of Washington, Seattle, Washington 98195, USA.
Leah HomadVaccine and Infectious Disease Division, Fred Hutchinson Cancer Research Center, Seattle, WA 98109.
Oliver ActonDepartment of Biochemistry, University of Washington, Seattle, Washington 98195, USA.
John BowenDepartment of Biochemistry, University of Washington, Seattle, Washington 98195, USA.
Chunyan WangVirology Division, Department of Infectious Diseases and Immunology, Faculty of Veterinary Medicine, Utrecht University, Utrecht, the Netherlands.
Xiaoli XiongDepartment of Biochemistry, University of Washington, Seattle, Washington 98195, USA.
Willem de van der SchuerenClinical Research Division, Fred Hutchinson Cancer Research Center, Seattle, WA, USA.
Joel QuispeDepartment of Biochemistry, University of Washington, Seattle, Washington 98195, USA.
Benjamin G HoffstromAntibody Technology Resource, Fred Hutchinson Cancer Research Center, Seattle, WA 98109.
Berend-Jan BoschVirology Division, Department of Infectious Diseases and Immunology, Faculty of Veterinary Medicine, Utrecht University, Utrecht, the Netherlands.
Andrew T McGuireVaccine and Infectious Disease Division, Fred Hutchinson Cancer Research Center, Seattle, WA 98109.
David VeeslerDepartment of Biochemistry, University of Washington, Seattle, Washington 98195, USA.
University of Washington · USFred Hutch Cancer Center · USUtrecht University · NLCentre National de la Recherche Scientifique · FR

Funding

Unraveling the bat humoral immune response against zoonotic viruses to guide the design of next-generation therapeuticsDP1AI158186 · NIAID · UNIVERSITY OF WASHINGTON · PI VEESLER, DAVID · 2020 to 2024
$5.4M
Structural Studies of Coronavirus Fusion ProteinsR01GM120553 · NIGMS · UNIVERSITY OF WASHINGTON · PI VEESLER, DAVID · 2016 to 2020
$1.7M
NIAID NIH HHS DP1 AI158186NIAID NIH HHS HHSN272201700059CNIGMS NIH HHS R01 GM120553
6 · The paper itself

Abstract

Three highly pathogenic β-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 β-coronavirus spike glycoproteins, including all five human-infecting β-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 β-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.

Identifiers

PMID33398277
PMCPMC7781312
OpenAlexW3116538810

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.