Evidence map›Paper›PMID 35981534›Full record

ArticleCell reports2022

A neutralizing epitope on the SD1 domain of SARS-CoV-2 spike targeted following infection and vaccination.

Jeffrey Seow, Hataf Khan, Annachiara Rosa, Valeria Calvaresi, Carl Graham, Suzanne Pickering, Valerie E Pye, Nora B Cronin, Isabella Huettner, Michael H Malim and 3 more

Open access · goldAbstract read
In one paragraph

Article in Cell reports, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
4.6field-weighted citation impact, top 4% 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

27 citing papers in PubMed, 47 citations in OpenAlex.

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  12. Production and Immunogenicity Assessment of LTp50: AnPharmaceuticals (Basel, Switzerland) · 2024
    Article
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  18. Broadly neutralizing antibodies against COVID-19.Current opinion in virology · 2023
    Review
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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

13 authors at 2 institutions in 1 country.

Jeffrey SeowDepartment of Infectious Diseases, School of Immunology & Microbial Sciences, King's College London, London, UK.
Hataf KhanDepartment of Infectious Diseases, School of Immunology & Microbial Sciences, King's College London, London, UK.
Annachiara RosaChromatin Structure and Mobile DNA Laboratory, The Francis Crick Institute, London, UK.
Valeria CalvaresiDepartment of Chemistry, King's College London, London, UK.
Carl GrahamDepartment of Infectious Diseases, School of Immunology & Microbial Sciences, King's College London, London, UK.
Suzanne PickeringDepartment of Infectious Diseases, School of Immunology & Microbial Sciences, King's College London, London, UK.
Valerie E PyeChromatin Structure and Mobile DNA Laboratory, The Francis Crick Institute, London, UK.
Nora B CroninLonCEM Facility, The Francis Crick Institute, London, UK.
Isabella HuettnerDepartment of Infectious Diseases, School of Immunology & Microbial Sciences, King's College London, London, UK.
Michael H MalimDepartment of Infectious Diseases, School of Immunology & Microbial Sciences, King's College London, London, UK.
Argyris PolitisDepartment of Chemistry, King's College London, London, UK. Electronic address: argyris.politis@kcl.ac.uk.
Peter CherepanovChromatin Structure and Mobile DNA Laboratory, The Francis Crick Institute, London, UK; Department of Infectious Disease, St-Mary's Campus, Imperial College London, London, UK. Electronic address: peter.cherepanov@crick.ac.uk.
Katie J DooresDepartment of Infectious Diseases, School of Immunology & Microbial Sciences, King's College London, London, UK. Electronic address: katie.doores@kcl.ac.uk.
King's College London · GBThe Francis Crick Institute · GB

Funding

Cancer Research UKMedical Research Council MR/N013700/1Medical Research Council MR/W005611/1Wellcome Trust 106223/Z/14/ZWellcome Trust 206175/Z/17/ZWellcome Trust 208354/Z/17/ZWellcome Trust 222433/Z/21/ZWellcome Trust FC001061
6 · The paper itself

Abstract

Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) spike is the target for neutralizing antibodies elicited following both infection and vaccination. While extensive research has shown that the receptor binding domain (RBD) and, to a lesser extent, the N-terminal domain (NTD) are the predominant targets for neutralizing antibodies, identification of neutralizing epitopes beyond these regions is important for informing vaccine development and understanding antibody-mediated immune escape. Here, we identify a class of broadly neutralizing antibodies that bind an epitope on the spike subdomain 1 (SD1) and that have arisen from infection or vaccination. Using cryo-electron microscopy (cryo-EM) and hydrogen-deuterium exchange coupled to mass spectrometry (HDX-MS), we show that SD1-specific antibody P008_60 binds an epitope that is not accessible within the canonical prefusion states of the SARS-CoV-2 spike, suggesting a transient conformation of the viral glycoprotein that is vulnerable to neutralization.

Indexed as

COVID-19SARS-CoV-2Antibodies, NeutralizingAntibodies, ViralCryoelectron MicroscopyEpitopesHumansNeutralization TestsSpike Glycoprotein, CoronavirusSyndactylyVaccinationAntibodies, NeutralizingAntibodies, ViralEpitopesSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2antibodyCP: ImmunologyCP: Microbiologycryogenic electron microscopyhydrogen-deuterium exchangeneutralizing epitopeomicronSARS-CoV-2spike subdomain 1

Identifiers

PMID35981534
PMCPMC9365860
OpenAlexW4292425691

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.