Evidence map›Paper›PMID 35857703›Full record

ArticleScience (New York, N.Y.)2022

ACE2-binding exposes the SARS-CoV-2 fusion peptide to broadly neutralizing coronavirus antibodies.

Jun Siong Low, Josipa Jerak, M Alejandra Tortorici, Matthew McCallum, Dora Pinto, Antonino Cassotta, Mathilde Foglierini, Federico Mele, Rana Abdelnabi, Birgit Weynand and 23 more

Open access · greenAbstract read
In one paragraph

Article in Science (New York, N.Y.), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 132 papers.

0numbers the graph read from it
0cells of the map it votes in
132citing papers in PubMed
17.3field-weighted citation impact, top 1% 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

132 citing papers in PubMed, 181 citations in OpenAlex.

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  12. TMPRSS2-mediated coronavirus spike activation and inhibition.Nature structural & molecular biology · 2026
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72 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

33 authors at 10 institutions in 5 countries.

Jun Siong Low *Institute for Research in Biomedicine, Università della Svizzera Italiana, 6500 Bellinzona, Switzerland.ORCID 0000-0002-1775-0778
Josipa Jerak *Institute for Research in Biomedicine, Università della Svizzera Italiana, 6500 Bellinzona, Switzerland.ORCID 0000-0001-5358-5055
M Alejandra Tortorici *Department of Biochemistry, University of Washington, Seattle, WA 98195, USA.ORCID 0000-0002-2260-2577
Matthew McCallum *Department of Biochemistry, University of Washington, Seattle, WA 98195, USA.ORCID 0000-0001-8398-8330
Dora Pinto *Humabs BioMed SA (subsidiary of Vir Biotechnology), 6500 Bellinzona, Switzerland.
Antonino CassottaInstitute for Research in Biomedicine, Università della Svizzera Italiana, 6500 Bellinzona, Switzerland.ORCID 0000-0001-8674-4294
Mathilde FoglieriniInstitute for Research in Biomedicine, Università della Svizzera Italiana, 6500 Bellinzona, Switzerland.ORCID 0000-0001-7538-4262
Federico MeleInstitute for Research in Biomedicine, Università della Svizzera Italiana, 6500 Bellinzona, Switzerland.ORCID 0000-0003-0455-4687
Rana AbdelnabiKU Leuven Department of Microbiology, Immunology and Transplantation, Rega Institute for Medical Research, Laboratory of Virology and Chemotherapy, B-3000 Leuven, Belgium.ORCID 0000-0001-9771-7312
Birgit WeynandKU Leuven Department of Imaging and Pathology, Translational Cell and Tissue Research, B-3000 Leuven, Belgium.ORCID 0000-0003-4246-6303
Julia NoackVir Biotechnology, San Francisco, CA 94158, USA.ORCID 0000-0002-9113-8181
Martin Montiel-RuizVir Biotechnology, San Francisco, CA 94158, USA.ORCID 0000-0001-6200-9578
Siro BianchiHumabs BioMed SA (subsidiary of Vir Biotechnology), 6500 Bellinzona, Switzerland.ORCID 0000-0002-5100-8905
Fabio BenigniHumabs BioMed SA (subsidiary of Vir Biotechnology), 6500 Bellinzona, Switzerland.ORCID 0000-0002-1974-5606
Nicole SprugasciHumabs BioMed SA (subsidiary of Vir Biotechnology), 6500 Bellinzona, Switzerland.ORCID 0000-0003-3258-5552
Anshu JoshiDepartment of Biochemistry, University of Washington, Seattle, WA 98195, USA.
John E BowenDepartment of Biochemistry, University of Washington, Seattle, WA 98195, USA.ORCID 0000-0003-3590-9727
Cameron StewartDepartment of Biochemistry, University of Washington, Seattle, WA 98195, USA.ORCID 0000-0002-2786-6256
Megi RexhepajDepartment of Biochemistry, University of Washington, Seattle, WA 98195, USA.ORCID 0000-0002-8107-7231
Alexandra C WallsDepartment of Biochemistry, University of Washington, Seattle, WA 98195, USA.ORCID 0000-0002-9636-8330
David JarrossayInstitute for Research in Biomedicine, Università della Svizzera Italiana, 6500 Bellinzona, Switzerland.ORCID 0000-0002-0924-6395
Diego MoroneInstitute for Research in Biomedicine, Università della Svizzera Italiana, 6500 Bellinzona, Switzerland.
Philipp PaparoditisInstitute for Research in Biomedicine, Università della Svizzera Italiana, 6500 Bellinzona, Switzerland.
Christian GarzoniClinic of Internal Medicine and Infectious Diseases, Clinica Luganese Moncucco, 6900 Lugano, Switzerland.ORCID 0000-0002-0832-2376
Paolo FerrariFaculty of Biomedical Sciences, Università della Svizzera Italiana, 6900 Lugano, Switzerland.ORCID 0000-0002-9619-3104
Alessandro CeschiFaculty of Biomedical Sciences, Università della Svizzera Italiana, 6900 Lugano, Switzerland.ORCID 0000-0002-4308-0405
Johan NeytsKU Leuven Department of Microbiology, Immunology and Transplantation, Rega Institute for Medical Research, Laboratory of Virology and Chemotherapy, B-3000 Leuven, Belgium.ORCID 0000-0002-0033-7514
Lisa A PurcellVir Biotechnology, San Francisco, CA 94158, USA.ORCID 0000-0002-9565-2030
Gyorgy SnellVir Biotechnology, San Francisco, CA 94158, USA.ORCID 0000-0003-1475-659X
Davide CortiHumabs BioMed SA (subsidiary of Vir Biotechnology), 6500 Bellinzona, Switzerland.ORCID 0000-0002-5797-1364
Antonio Lanzavecchia *Humabs BioMed SA (subsidiary of Vir Biotechnology), 6500 Bellinzona, Switzerland.ORCID 0000-0002-3041-7240
David Veesler *Department of Biochemistry, University of Washington, Seattle, WA 98195, USA.ORCID 0000-0002-6019-8675
Federica Sallusto *Institute for Research in Biomedicine, Università della Svizzera Italiana, 6500 Bellinzona, Switzerland.ORCID 0000-0003-3750-2752
Università della Svizzera italiana · CHUniversity of Washington · USVir Biotechnology (Switzerland) · CHVIR Biotechnology (United States) · USETH Zurich · CHEnte Ospedaliero Cantonale · CHHoward Hughes Medical Institute · USRega Institute for Medical Research · BEClinica Luganese Moncucco · CHKU Leuven · BE

Funding

A Synchrotron Radiation Structural Biology ResourcesP30GM133894 · NIGMS · STANFORD UNIVERSITY · PI Aina E. Cohen, KEITH O HODGSON · 2020 to 2026
$43.3M
User Training & OutreachP30GM138396 · NIGMS · UCHICAGO ARGONNE, LLC · PI ROBERT F. FISCHETTI · 2020 to 2026
$34.3M
Germline targeting influenza immunogensR01AI132317 · NIAID · SCRIPPS RESEARCH INSTITUTE, THE · PI NEMAZEE, DAVID · 2017 to 2021
$7.0M
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
NIAID NIH HHS DP1 AI158186NIAID NIH HHS HHSN272201700059CNIAID NIH HHS R01 AI132317NIGMS NIH HHS P30 GM133894NIGMS NIH HHS P30 GM138396
6 · The paper itself

Abstract

The coronavirus spike glycoprotein attaches to host receptors and mediates viral fusion. Using a broad screening approach, we isolated seven monoclonal antibodies (mAbs) that bind to all human-infecting coronavirus spike proteins from severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) immune donors. These mAbs recognize the fusion peptide and acquire affinity and breadth through somatic mutations. Despite targeting a conserved motif, only some mAbs show broad neutralizing activity in vitro against alpha- and betacoronaviruses, including animal coronaviruses WIV-1 and PDF-2180. Two selected mAbs also neutralize Omicron BA.1 and BA.2 authentic viruses and reduce viral burden and pathology in vivo. Structural and functional analyses showed that the fusion peptide-specific mAbs bound with different modalities to a cryptic epitope hidden in prefusion stabilized spike, which became exposed upon binding of angiotensin-converting enzyme 2 (ACE2) or ACE2-mimicking mAbs.

Indexed as

Angiotensin-Converting Enzyme 2Antibodies, MonoclonalAntibodies, ViralBroadly Neutralizing AntibodiesCOVID-19SARS-CoV-2Spike Glycoprotein, CoronavirusAnimalsHumansPeptidesProtein BindingAngiotensin-Converting Enzyme 2Antibodies, MonoclonalAntibodies, ViralBroadly Neutralizing AntibodiesPeptidesSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2

Identifiers

PMID35857703
PMCPMC9348755
OpenAlexW4285041350

What OpenQuestion holds

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Registered trials

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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.