Evidence map›Paper›PMID 32700671›Full record

ArticleEuro surveillance : bulletin Europeen sur les maladies transmissibles = European communicable disease bulletin2020

Monoclonal antibodies for the S2 subunit of spike of SARS-CoV-1 cross-react with the newly-emerged SARS-CoV-2.

Zhiqiang Zheng, Vanessa Marthe Monteil, Sebastian Maurer-Stroh, Chow Wenn Yew, Carol Leong, Nur Khairiah Mohd-Ismail, Suganya Cheyyatraivendran Arularasu, Vincent Tak Kwong Chow, Raymond Tzer Pin Lin, Ali Mirazimi and 2 more

Open access · diamondAbstract read
In one paragraph

Article in Euro surveillance : bulletin Europeen sur les maladies transmissibles = European communicable disease bulletin, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed, 1 pooled it
2.0field-weighted citation impact, top 7% 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

63 citing papers in PubMed, 1 synthesis or guideline pooled it, 85 citations in OpenAlex.

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  17. SARS-CoV-2 Spike Protein and Mouse Coronavirus Inhibit Biofilm Formation byInternational journal of molecular sciences · 2022
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  20. Structural biology of SARS-CoV-2: open the door for novel therapies.Signal transduction and targeted therapy · 2022
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3 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

12 authors at 3 institutions in 2 countries.

Zhiqiang ZhengInfectious Diseases programme, Department of Microbiology and Immunology, Yong Loo Lin School of Medicine, National University Health System (NUHS), National University of Singapore, Singapore.
Vanessa Marthe MonteilDepartment of Laboratory Medicine, Karolinska Institute, Huddinge, Sweden.
Sebastian Maurer-StrohBioinformatics Institute (BII), A*STAR (Agency for Science, Technology and Research), Singapore.
Chow Wenn YewInstitute of Molecular and Cell Biology (IMCB), A*STAR (Agency for Science, Technology and Research), Singapore.
Carol LeongInstitute of Molecular and Cell Biology (IMCB), A*STAR (Agency for Science, Technology and Research), Singapore.
Nur Khairiah Mohd-IsmailInfectious Diseases programme, Department of Microbiology and Immunology, Yong Loo Lin School of Medicine, National University Health System (NUHS), National University of Singapore, Singapore.
Suganya Cheyyatraivendran ArularasuInfectious Diseases programme, Department of Microbiology and Immunology, Yong Loo Lin School of Medicine, National University Health System (NUHS), National University of Singapore, Singapore.
Vincent Tak Kwong ChowInfectious Diseases programme, Department of Microbiology and Immunology, Yong Loo Lin School of Medicine, National University Health System (NUHS), National University of Singapore, Singapore.
Raymond Tzer Pin LinNational Public Health Laboratory (NPHL), National Centre for Infectious Diseases (NCID), Singapore.
Ali MirazimiNational Veterinary Institute, Uppsala, Sweden.
Wanjin HongInstitute of Molecular and Cell Biology (IMCB), A*STAR (Agency for Science, Technology and Research), Singapore.
Yee-Joo TanInfectious Diseases programme, Department of Microbiology and Immunology, Yong Loo Lin School of Medicine, National University Health System (NUHS), National University of Singapore, Singapore.
Agency for Science, Technology and Research · SGNational University of Singapore · SGPublic Health Agency of Sweden · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

BackgroundA novel coronavirus, SARS-CoV-2, which emerged at the end of 2019 and causes COVID-19, has resulted in worldwide human infections. While genetically distinct, SARS-CoV-1, the aetiological agent responsible for an outbreak of severe acute respiratory syndrome (SARS) in 2002-2003, utilises the same host cell receptor as SARS-CoV-2 for entry: angiotensin-converting enzyme 2 (ACE2). Parts of the SARS-CoV-1 spike glycoprotein (S protein), which interacts with ACE2, appear conserved in SARS-CoV-2.AimThe cross-reactivity with SARS-CoV-2 of monoclonal antibodies (mAbs) previously generated against the S protein of SARS-CoV-1 was assessed.MethodsThe SARS-CoV-2 S protein sequence was aligned to those of SARS-CoV-1, Middle East respiratory syndrome (MERS) and common-cold coronaviruses. Abilities of mAbs generated against SARS-CoV-1 S protein to bind SARS-CoV-2 or its S protein were tested with SARS-CoV-2 infected cells as well as cells expressing either the full length protein or a fragment of its S2 subunit. Quantitative ELISA was also performed to compare binding of mAbs to recombinant S protein.ResultsAn immunogenic domain in the S2 subunit of SARS-CoV-1 S protein is highly conserved in SARS-CoV-2 but not in MERS and human common-cold coronaviruses. Four murine mAbs raised against this immunogenic fragment could recognise SARS-CoV-2 S protein expressed in mammalian cell lines. In particular, mAb 1A9 was demonstrated to detect S protein in SARS-CoV-2-infected cells and is suitable for use in a sandwich ELISA format.ConclusionThe cross-reactive mAbs may serve as useful tools for SARS-CoV-2 research and for the development of diagnostic assays for COVID-19.

Indexed as

Amino Acid SequenceAngiotensin-Converting Enzyme 2AnimalsAntibodies, MonoclonalBetacoronavirusBlotting, WesternChlorocebus aethiopsConserved SequenceCoronavirus InfectionsCOS CellsCOVID-19Cross ReactionsEnzyme-Linked Immunosorbent AssayFluorescent Antibody TechniqueGenome, ViralMiceACE2 protein, humanAce2 protein, mouseAngiotensin-Converting Enzyme 2Antibodies, MonoclonalPeptidyl-Dipeptidase ARecombinant ProteinsSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2coronavirus disease 2019COVID-19cross-reactive antibodiesSARS-CoV-2spike protein

Identifiers

PMID32700671
PMCPMC7376845
OpenAlexW3042940033

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.