Evidence map›Paper›PMID 33114742›Full record

ArticleViruses2020

Antibody Binding to SARS-CoV-2 S Glycoprotein Correlates with but Does Not Predict Neutralization.

Shilei Ding, Annemarie Laumaea, Mehdi Benlarbi, Guillaume Beaudoin-Bussières, Romain Gasser, Halima Medjahed, Marie Pancera, Leonidas Stamatatos, Andrew T McGuire, Renée Bazin and 1 more

Open access · goldAbstract read
In one paragraph

Article in Viruses, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed, 1 pooled it
0.8field-weighted citation impact, top 16% 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

25 citing papers in PubMed, 1 synthesis or guideline pooled it, 32 citations in OpenAlex.

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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

11 authors at 4 institutions in 2 countries.

Shilei DingCentre de Recherche du CHUM, Montréal, QC H2X 0A9, Canada.
Annemarie LaumaeaCentre de Recherche du CHUM, Montréal, QC H2X 0A9, Canada.
Mehdi BenlarbiCentre de Recherche du CHUM, Montréal, QC H2X 0A9, Canada.
Guillaume Beaudoin-BussièresCentre de Recherche du CHUM, Montréal, QC H2X 0A9, Canada.
Romain GasserCentre de Recherche du CHUM, Montréal, QC H2X 0A9, Canada.
Halima MedjahedCentre de Recherche du CHUM, Montréal, QC H2X 0A9, Canada.
Marie PanceraFred Hutchinson Cancer Research Center, Vaccines and Infectious Diseases Division, Seattle, WA 98109, USA.
Leonidas StamatatosFred Hutchinson Cancer Research Center, Vaccines and Infectious Diseases Division, Seattle, WA 98109, USA.
Andrew T McGuireFred Hutchinson Cancer Research Center, Vaccines and Infectious Diseases Division, Seattle, WA 98109, USA.
Renée BazinHéma-Québec, Affaires Médicales et Innovation, Québec, QC G1V 5C3, Canada.
Andrés FinziCentre de Recherche du CHUM, Montréal, QC H2X 0A9, Canada.
Centre Hospitalier de l’Université de Montréal · CAUniversity of Washington · USFred Hutch Cancer Center · USHéma-Québec · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Convalescent plasma from SARS-CoV-2 infected individuals and monoclonal antibodies were shown to potently neutralize viral and pseudoviral particles carrying the S glycoprotein. However, a non-negligent proportion of plasma samples from infected individuals, as well as S-specific monoclonal antibodies, were reported to be non-neutralizing despite efficient interaction with the S glycoprotein in different biochemical assays using soluble recombinant forms of S or when expressed at the cell surface. How neutralization relates to the binding of S glycoprotein in the context of viral particles remains to be established. Here, we developed a pseudovirus capture assay (VCA) to measure the capacity of plasma samples or antibodies immobilized on ELISA plates to bind to membrane-bound S glycoproteins from SARS-CoV-2 expressed at the surface of lentiviral particles. By performing VCA, ELISA, and neutralization assays, we observed a strong correlation between these parameters. However, while we found that plasma samples unable to capture viral particles did not neutralize, capture did not guarantee neutralization, indicating that the capacity of antibodies to bind to the S glycoprotein at the surface of pseudoviral particles is required but not sufficient to mediate neutralization. Altogether, our results highlight the importance of better understanding the inactivation of S by plasma and neutralizing antibodies.

Indexed as

AnimalsAntibodies, ImmobilizedAntibodies, MonoclonalAntibodies, NeutralizingAntibodies, ViralBetacoronavirusCell LineConvalescenceCoronavirus InfectionsCOVID-19HEK293 CellsHumansNeutralization TestsPandemicsPneumonia, ViralSARS-CoV-2Antibodies, ImmobilizedAntibodies, MonoclonalAntibodies, NeutralizingAntibodies, ViralSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2convalescent plasmaCOVID-19ELISAneutralizationSARS-COV-2virus capture assay

Identifiers

PMID33114742
PMCPMC7692607
OpenAlexW3096248042

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.