Evidence map›Paper›PMID 32870820›Full record

ArticleJCI insight2020

A simple protein-based surrogate neutralization assay for SARS-CoV-2.

Kento T Abe, Zhijie Li, Reuben Samson, Payman Samavarchi-Tehrani, Emelissa J Valcourt, Heidi Wood, Patrick Budylowski, Alan P Dupuis, Roxie C Girardin, Bhavisha Rathod and 13 more

Open access · goldAbstract read
In one paragraph

Article in JCI insight, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 142 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
142citing papers in PubMed, 2 pooled it
5.2field-weighted citation impact, top 3% 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

142 citing papers in PubMed, 2 syntheses or guidelines pooled it, 236 citations in OpenAlex.

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82 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

23 authors at 8 institutions in 2 countries.

Kento T AbeDepartment of Molecular Genetics, University of Toronto, Toronto, Ontario, Canada.
Zhijie LiDepartment of Molecular Genetics, University of Toronto, Toronto, Ontario, Canada.
Reuben SamsonDepartment of Molecular Genetics, University of Toronto, Toronto, Ontario, Canada.
Payman Samavarchi-TehraniLunenfeld-Tanenbaum Research Institute at Mount Sinai Hospital, Sinai Health System, Toronto, Ontario, Canada.
Emelissa J ValcourtZoonotic Diseases and Special Pathogens, National Microbiology Laboratory (NML), Public Health Agency of Canada, Winnipeg, Manitoba, Canada.
Heidi WoodZoonotic Diseases and Special Pathogens, National Microbiology Laboratory (NML), Public Health Agency of Canada, Winnipeg, Manitoba, Canada.
Patrick BudylowskiDepartment of Immunology and.
Alan P DupuisWadsworth Center, New York State Department of Health, Albany, New York, USA.
Roxie C GirardinWadsworth Center, New York State Department of Health, Albany, New York, USA.
Bhavisha RathodLunenfeld-Tanenbaum Research Institute at Mount Sinai Hospital, Sinai Health System, Toronto, Ontario, Canada.
Jenny H WangLunenfeld-Tanenbaum Research Institute at Mount Sinai Hospital, Sinai Health System, Toronto, Ontario, Canada.
Miriam Barrios-RodilesLunenfeld-Tanenbaum Research Institute at Mount Sinai Hospital, Sinai Health System, Toronto, Ontario, Canada.
Karen ColwillLunenfeld-Tanenbaum Research Institute at Mount Sinai Hospital, Sinai Health System, Toronto, Ontario, Canada.
Allison J McGeerLunenfeld-Tanenbaum Research Institute at Mount Sinai Hospital, Sinai Health System, Toronto, Ontario, Canada.
Samira MubarekaDepartment of Laboratory Medicine and Molecular Diagnostics, Division of Microbiology, Sunnybrook Health Sciences Centre, Toronto, Ontario, Canada.
Jennifer L GommermanDepartment of Immunology and.
Yves DurocherMammalian Cell Expression, Human Health Therapeutics Research Centre, National Research Council Canada, Montréal, Quebec, Canada.
Mario OstrowskiDepartment of Immunology and.
Kathleen A McDonoughWadsworth Center, New York State Department of Health, Albany, New York, USA.
Michael A DrebotZoonotic Diseases and Special Pathogens, National Microbiology Laboratory (NML), Public Health Agency of Canada, Winnipeg, Manitoba, Canada.
Steven J DrewsCanadian Blood Services, Edmonton, AB & Department of Laboratory Medicine and Pathology, University of Alberta, Edmonton, Alberta, Canada.
James M RiniDepartment of Molecular Genetics, University of Toronto, Toronto, Ontario, Canada.
Anne-Claude GingrasDepartment of Molecular Genetics, University of Toronto, Toronto, Ontario, Canada.
Mount Sinai Hospital · CANew York State Department of Health · USPublic Health Agency of Canada · CAUniversity of Toronto · CACanadian Blood Services · CANational Research Council Canada · CASt. Michael's Hospital · CASunnybrook Health Science Centre · CA

Funding

NIAID NIH HHS HHSN272201400008C
6 · The paper itself

Abstract

Most of the patients infected with severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) mount a humoral immune response to the virus within a few weeks of infection, but the duration of this response and how it correlates with clinical outcomes has not been completely characterized. Of particular importance is the identification of immune correlates of infection that would support public health decision-making on treatment approaches, vaccination strategies, and convalescent plasma therapy. While ELISA-based assays to detect and quantitate antibodies to SARS-CoV-2 in patient samples have been developed, the detection of neutralizing antibodies typically requires more demanding cell-based viral assays. Here, we present a safe and efficient protein-based assay for the detection of serum and plasma antibodies that block the interaction of the SARS-CoV-2 spike protein receptor binding domain (RBD) with its receptor, angiotensin-converting enzyme 2 (ACE2). The assay serves as a surrogate neutralization assay and is performed on the same platform and in parallel with an ELISA for the detection of antibodies against the RBD, enabling a direct comparison. The results obtained with our assay correlate with those of 2 viral-based assays, a plaque reduction neutralization test (PRNT) that uses live SARS-CoV-2 virus and a spike pseudotyped viral vector-based assay.

Indexed as

Antibodies, NeutralizingAntibodies, ViralArea Under CurveCoronavirus InfectionsCOVID-19COVID-19 SerotherapyEnzyme-Linked Immunosorbent AssayHumansImmunization, PassiveNeutralization TestsPandemicsPneumonia, ViralRegression AnalysisSampling StudiesSpike Glycoprotein, CoronavirusTreatment OutcomeAntibodies, NeutralizingAntibodies, ViralSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2Viral Envelope ProteinsAdaptive immunityAntigenImmunoglobulinsInfectious disease

Identifiers

PMID32870820
PMCPMC7566699
OpenAlexW3082734312

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.