Evidence map›Paper›PMID 35411021›Full record

ArticleCommunications biology2022

Structural definition of a pan-sarbecovirus neutralizing epitope on the spike S2 subunit.

Nicholas K Hurlburt, Leah J Homad, Irika Sinha, Madeleine F Jennewein, Anna J MacCamy, Yu-Hsin Wan, Jim Boonyaratanakornkit, Anton M Sholukh, Abigail M Jackson, Panpan Zhou and 7 more

Open access · goldAbstract read
In one paragraph

Article in Communications biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.

0numbers the graph read from it
0cells of the map it votes in
68citing papers in PubMed
7.8field-weighted citation impact, top 2% of its field
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

68 citing papers in PubMed, 86 citations in OpenAlex.

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  14. Molecular mechanisms of SARS-CoV-2 entry: implications for biomedical strategies.Microbiology and molecular biology reviews : MMBR · 2025
    Review
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8 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

17 authors at 4 institutions in 2 countries.

Nicholas K Hurlburt *Fred Hutchinson Cancer Research Center, Vaccine and Infectious Disease Division, Seattle, WA, USA.ORCID 0000-0001-9891-916X
Leah J Homad *Fred Hutchinson Cancer Research Center, Vaccine and Infectious Disease Division, Seattle, WA, USA.ORCID 0000-0001-8421-6519
Irika SinhaFred Hutchinson Cancer Research Center, Vaccine and Infectious Disease Division, Seattle, WA, USA.ORCID 0000-0001-6440-7019
Madeleine F JenneweinFred Hutchinson Cancer Research Center, Vaccine and Infectious Disease Division, Seattle, WA, USA.
Anna J MacCamyFred Hutchinson Cancer Research Center, Vaccine and Infectious Disease Division, Seattle, WA, USA.
Yu-Hsin WanFred Hutchinson Cancer Research Center, Vaccine and Infectious Disease Division, Seattle, WA, USA.
Jim BoonyaratanakornkitFred Hutchinson Cancer Research Center, Vaccine and Infectious Disease Division, Seattle, WA, USA.ORCID 0000-0001-5858-2662
Anton M SholukhFred Hutchinson Cancer Research Center, Vaccine and Infectious Disease Division, Seattle, WA, USA.ORCID 0000-0003-0498-9162
Abigail M JacksonDepartment of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA, USA.ORCID 0000-0001-9749-9431
Panpan ZhouDepartment of Immunology and Microbiology, The Scripps Research Institute, La Jolla, CA, USA.ORCID 0000-0001-5740-4303
Dennis R BurtonDepartment of Immunology and Microbiology, The Scripps Research Institute, La Jolla, CA, USA.ORCID 0000-0001-6711-9864
Raiees AndrabiDepartment of Immunology and Microbiology, The Scripps Research Institute, La Jolla, CA, USA.ORCID 0000-0001-8837-7520
Gabriel OzorowskiDepartment of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA, USA.ORCID 0000-0002-9695-8138
Andrew B WardDepartment of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA, USA.ORCID 0000-0001-7153-3769
Leonidas StamatatosFred Hutchinson Cancer Research Center, Vaccine and Infectious Disease Division, Seattle, WA, USA. lstamata@fredhutch.org.ORCID 0000-0002-1106-7097
Marie PanceraFred Hutchinson Cancer Research Center, Vaccine and Infectious Disease Division, Seattle, WA, USA. mpancera@fredhutch.org.ORCID 0000-0001-9217-6270
Andrew T McGuireFred Hutchinson Cancer Research Center, Vaccine and Infectious Disease Division, Seattle, WA, USA. amcguire@fredhutch.org.ORCID 0000-0003-1841-6859
Fred Hutch Cancer Center · USScripps Research Institute · USCape Town HVTN Immunology Laboratory / Hutchinson Centre Research Institute of South Africa · ZANational Institutes of Health · US

Funding

Identification of neutralizing epitopes on SARS-CoV-2 spike for design of vaccines and small-molecule antiviralsUM1AI144462 · NIAID · SCRIPPS RESEARCH INSTITUTE, THE · PI BURTON, DENNIS R. · 2019 to 2025
$201.6M
Howard Hughes Medical InstituteNIAID NIH HHS UM1 AI144462
6 · The paper itself

Abstract

Three betacoronaviruses have crossed the species barrier and established human-to-human transmission causing significant morbidity and mortality in the past 20 years. The most current and widespread of these is SARS-CoV-2. The identification of CoVs with zoonotic potential in animal reservoirs suggests that additional outbreaks could occur. Monoclonal antibodies targeting conserved neutralizing epitopes on diverse CoVs can form the basis for prophylaxis and therapeutic treatments and enable the design of vaccines aimed at providing pan-CoV protection. We previously identified a neutralizing monoclonal antibody, CV3-25 that binds to the SARS-CoV-2 spike, neutralizes the SARS-CoV-2 Beta variant comparably to the ancestral Wuhan Hu-1 strain, cross neutralizes SARS-CoV-1 and binds to recombinant proteins derived from the spike-ectodomains of HCoV-OC43 and HCoV-HKU1. Here, we show that the neutralizing activity of CV3-25 is maintained against the Alpha, Delta, Gamma and Omicron variants of concern as well as a SARS-CoV-like bat coronavirus with zoonotic potential by binding to a conserved linear peptide in the stem-helix region. Negative stain electron microscopy and a 1.74 Å crystal structure of a CV3-25/peptide complex demonstrates that CV3-25 binds to the base of the stem helix at the HR2 boundary to an epitope that is distinct from other stem-helix directed neutralizing mAbs.

Indexed as

COVID-19SARS-CoV-2AnimalsAntibodies, MonoclonalAntibodies, NeutralizingAntibodies, ViralEpitopesSpike Glycoprotein, CoronavirusAntibodies, MonoclonalAntibodies, NeutralizingAntibodies, ViralEpitopesSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2

Identifiers

PMID35411021
PMCPMC9001700
OpenAlexW4226077400

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.