Evidence map›Paper›PMID 33821273›Full record

ArticlebioRxiv : the preprint server for biology2022

A human antibody reveals a conserved site on beta-coronavirus spike proteins and confers protection against SARS-CoV-2 infection.

Panpan Zhou, Meng Yuan, Ge Song, Nathan Beutler, Namir Shaabani, Deli Huang, Wan-Ting He, Xueyong Zhu, Sean Callaghan, Peter Yong and 13 more

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

Article in bioRxiv : the preprint server for biology, 2022. 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, 54 citations in OpenAlex.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

23 authors at 2 institutions in 1 country.

Panpan ZhouDepartment of Immunology and Microbiology, The Scripps Research Institute, La Jolla, CA 92037, USA.
Meng YuanDepartment of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
Ge SongDepartment of Immunology and Microbiology, The Scripps Research Institute, La Jolla, CA 92037, USA.
Nathan BeutlerDepartment of Immunology and Microbiology, The Scripps Research Institute, La Jolla, CA 92037, USA.
Namir ShaabaniDepartment of Immunology and Microbiology, The Scripps Research Institute, La Jolla, CA 92037, USA.
Deli HuangDepartment of Immunology and Microbiology, The Scripps Research Institute, La Jolla, CA 92037, USA.
Wan-Ting HeDepartment of Immunology and Microbiology, The Scripps Research Institute, La Jolla, CA 92037, USA.
Xueyong ZhuDepartment of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
Sean CallaghanDepartment of Immunology and Microbiology, The Scripps Research Institute, La Jolla, CA 92037, USA.
Peter YongDepartment of Immunology and Microbiology, The Scripps Research Institute, La Jolla, CA 92037, USA.
Fabio AnzanelloDepartment of Immunology and Microbiology, The Scripps Research Institute, La Jolla, CA 92037, USA.
Linghang PengDepartment of Immunology and Microbiology, The Scripps Research Institute, La Jolla, CA 92037, USA.
James RickettsDepartment of Immunology and Microbiology, The Scripps Research Institute, La Jolla, CA 92037, USA.
Mara ParrenDepartment of Immunology and Microbiology, The Scripps Research Institute, La Jolla, CA 92037, USA.
Elijah GarciaDepartment of Immunology and Microbiology, The Scripps Research Institute, La Jolla, CA 92037, USA.
Stephen A RawlingsDivision of Infectious Diseases, Department of Medicine, University of California, San Diego, La Jolla, CA 92037, USA.
Davey M SmithDivision of Infectious Diseases, Department of Medicine, University of California, San Diego, La Jolla, CA 92037, USA.
David NemazeeDepartment of Immunology and Microbiology, The Scripps Research Institute, La Jolla, CA 92037, USA.
John R TeijaroDepartment of Immunology and Microbiology, The Scripps Research Institute, La Jolla, CA 92037, USA.
Thomas F RogersDepartment of Immunology and Microbiology, The Scripps Research Institute, La Jolla, CA 92037, USA.
Ian A WilsonDepartment of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
Dennis R BurtonDepartment of Immunology and Microbiology, The Scripps Research Institute, La Jolla, CA 92037, USA.
Raiees AndrabiDepartment of Immunology and Microbiology, The Scripps Research Institute, La Jolla, CA 92037, USA.
Scripps Research Institute · USUniversity of California San Diego · US

Funding

VirologyP30AI036214 · NIAID · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI David Mitchell Smith · 1994 to 2026
$78.4M
ZWITTERION SURFACTANT DDMAB FOR IMPROV STABIL OF PROTEINP41RR001209 · NCRR · STANFORD UNIVERSITY · PI SCOTT, EMILY E · 1985 to 2011
$38.9M
X-ray Absorption Spectroscopy (XAS) pp.711-759P41GM103393 · NIGMS · STANFORD UNIVERSITY · PI HODGSON, KEITH O · 2012 to 2019
$30.6M
HOPE Training GrantT32AI007384 · NIAID · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI Sara Gianella Weibel, Scott L Letendre · 1990 to 2026
$9.7M
NCRR NIH HHS P41 RR001209NIAID NIH HHS P30 AI036214NIAID NIH HHS T32 AI007384NIGMS NIH HHS P41 GM103393
6 · The paper itself

Abstract

Broadly neutralizing antibodies (bnAbs) to coronaviruses (CoVs) are valuable in their own right as prophylactic and therapeutic reagents to treat diverse CoVs and, importantly, as templates for rational pan-CoV vaccine design. We recently described a bnAb, CC40.8, from a coronavirus disease 2019 (COVID-19)-convalescent donor that exhibits broad reactivity with human beta-coronaviruses (β-CoVs). Here, we showed that CC40.8 targets the conserved S2 stem-helix region of the coronavirus spike fusion machinery. We determined a crystal structure of CC40.8 Fab with a SARS-CoV-2 S2 stem-peptide at 1.6 Å resolution and found that the peptide adopted a mainly helical structure. Conserved residues in β-CoVs interacted with CC40.8 antibody, thereby providing a molecular basis for its broad reactivity. CC40.8 exhibited in vivo protective efficacy against SARS-CoV-2 challenge in two animal models. In both models, CC40.8-treated animals exhibited less weight loss and reduced lung viral titers compared to controls. Furthermore, we noted CC40.8-like bnAbs are relatively rare in human COVID-19 infection and therefore their elicitation may require rational structure-based vaccine design strategies. Overall, our study describes a target on β-CoV spike proteins for protective antibodies that may facilitate the development of pan-β-CoV vaccines. SUMMARY: A human mAb isolated from a COVID-19 donor defines a protective cross-neutralizing epitope for pan-β-CoV vaccine design strategies.

Identifiers

PMID33821273
PMCPMC8020973
OpenAlexW3146780841

What OpenQuestion holds

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LicenceCC BY-NC-ND
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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.