Evidence map›Paper›PMID 32245784›Full record

ArticleScience (New York, N.Y.)2020

A highly conserved cryptic epitope in the receptor binding domains of SARS-CoV-2 and SARS-CoV.

Meng Yuan, Nicholas C Wu, Xueyong Zhu, Chang-Chun D Lee, Ray T Y So, Huibin Lv, Chris K P Mok, Ian A Wilson

Open access · hybridAbstract read
In one paragraph

Article in Science (New York, N.Y.), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1,043 papers.

0numbers the graph read from it
0cells of the map it votes in
1,043citing papers in PubMed
37.6field-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

1,043 citing papers in PubMed, 1,661 citations in OpenAlex.

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  16. D614G reshapes allosteric networks and opening mechanisms of SARS-CoV-2 spikes.Proceedings of the National Academy of Sciences of the United States of America · 2026
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983 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

8 authors at 2 institutions in 2 countries.

Meng Yuan *Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.ORCID 0000-0001-9754-4503
Nicholas C Wu *Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.ORCID 0000-0002-9078-6697
Xueyong ZhuDepartment of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.ORCID 0000-0002-6021-3740
Chang-Chun D LeeDepartment of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.ORCID 0000-0002-5470-2484
Ray T Y SoHKU-Pasteur Research Pole, School of Public Health, Li Ka Shing Faculty of Medicine, The University of Hong Kong, Hong Kong SAR, China.ORCID 0000-0002-9576-4489
Huibin LvHKU-Pasteur Research Pole, School of Public Health, Li Ka Shing Faculty of Medicine, The University of Hong Kong, Hong Kong SAR, China.ORCID 0000-0003-2218-0076
Chris K P MokHKU-Pasteur Research Pole, School of Public Health, Li Ka Shing Faculty of Medicine, The University of Hong Kong, Hong Kong SAR, China. ch02mkp@hku.hk wilson@scripps.edu.ORCID 0000-0002-0525-6772
Ian A WilsonDepartment of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA. ch02mkp@hku.hk wilson@scripps.edu.ORCID 0000-0002-6469-2419
Scripps Research Institute · USHKU-Pasteur Research Pole · HK

Funding

Mechanistic understanding of influenza-host interactions from a zoonotic perspectiveK99AI139445 · NIAID · SCRIPPS RESEARCH INSTITUTE, THE · PI WU, NICHOLAS C. · 2019 to 2020
$132k
NIAID NIH HHS K99 AI139445
6 · The paper itself

Abstract

The outbreak of coronavirus disease 2019 (COVID-19) caused by severe acute respiratory syndrome-coronavirus 2 (SARS-CoV-2) has now become a pandemic, but there is currently very little understanding of the antigenicity of the virus. We therefore determined the crystal structure of CR3022, a neutralizing antibody previously isolated from a convalescent SARS patient, in complex with the receptor binding domain (RBD) of the SARS-CoV-2 spike (S) protein at 3.1-angstrom resolution. CR3022 targets a highly conserved epitope, distal from the receptor binding site, that enables cross-reactive binding between SARS-CoV-2 and SARS-CoV. Structural modeling further demonstrates that the binding epitope can only be accessed by CR3022 when at least two RBDs on the trimeric S protein are in the "up" conformation and slightly rotated. These results provide molecular insights into antibody recognition of SARS-CoV-2.

Indexed as

EpitopesAmino Acid SequenceAngiotensin-Converting Enzyme 2Antibodies, NeutralizingAntibodies, ViralAntibody AffinityAntigens, ViralBetacoronavirusBinding SitesCross ReactionsCrystallography, X-RayModels, MolecularPeptidyl-Dipeptidase AProtein ConformationProtein DomainsProtein Interaction Domains and MotifsAngiotensin-Converting Enzyme 2Antibodies, NeutralizingAntibodies, ViralAntigens, ViralEpitopesPeptidyl-Dipeptidase AReceptors, CoronavirusReceptors, VirusSpike Glycoprotein, Coronavirusspike glycoprotein, SARS-CoVspike protein, SARS-CoV-2

Identifiers

PMID32245784
PMCPMC7164391
OpenAlexW3014656992

What OpenQuestion holds

Textmetadata
LicenceTDM
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.