Evidence map›Paper›PMID 36916782›Full record

ArticleJournal of medical virology2023

Distinct in vitro and in vivo neutralization profiles of monoclonal antibodies elicited by the receptor binding domain of the ancestral SARS-CoV-2.

Hyung J Kwon, Jun Zhang, Matina Kosikova, Weichun Tang, Uriel Ortega-Rodriguez, Hanqin Peng, Clement A Meseda, Cyntia L Pedro, Falko Schmeisser, Jianming Lu and 11 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of medical virology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

2 citing papers in PubMed.

  1. Viral syncytia evolve to resist interferon.Nature communications · 2026
    Article
  2. Article
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

21 authors.

Hyung J KwonLaboratory of Pediatric and Respiratory Viral Diseases, Division of Viral Products, Center for Biologics Evaluation and Research, Office of Vaccines Research and Review, United States Food and Drug Administration, Silver Spring, Maryland, USA.
Jun ZhangDivision of Molecular Medicine, Boston Children's Hospital, Boston, Massachusetts, USA.
Matina KosikovaLaboratory of Pediatric and Respiratory Viral Diseases, Division of Viral Products, Center for Biologics Evaluation and Research, Office of Vaccines Research and Review, United States Food and Drug Administration, Silver Spring, Maryland, USA.
Weichun TangLaboratory of Pediatric and Respiratory Viral Diseases, Division of Viral Products, Center for Biologics Evaluation and Research, Office of Vaccines Research and Review, United States Food and Drug Administration, Silver Spring, Maryland, USA.
Uriel Ortega-RodriguezLaboratory of Pediatric and Respiratory Viral Diseases, Division of Viral Products, Center for Biologics Evaluation and Research, Office of Vaccines Research and Review, United States Food and Drug Administration, Silver Spring, Maryland, USA.ORCID 0000-0002-1700-357X
Hanqin PengDivision of Molecular Medicine, Boston Children's Hospital, Boston, Massachusetts, USA.
Clement A MesedaLaboratory of DNA viruses, Division of Viral Products, Center for Biologics Evaluation and Research, Office of Vaccines Research and Review, United States Food and Drug Administration, Silver Spring, Maryland, USA.
Cyntia L PedroLaboratory of DNA viruses, Division of Viral Products, Center for Biologics Evaluation and Research, Office of Vaccines Research and Review, United States Food and Drug Administration, Silver Spring, Maryland, USA.
Falko SchmeisserLaboratory of DNA viruses, Division of Viral Products, Center for Biologics Evaluation and Research, Office of Vaccines Research and Review, United States Food and Drug Administration, Silver Spring, Maryland, USA.
Jianming LuCodex BioSolutions, Inc., Rockville, Maryland, USA.
Insung KangLaboratory of Pediatric and Respiratory Viral Diseases, Division of Viral Products, Center for Biologics Evaluation and Research, Office of Vaccines Research and Review, United States Food and Drug Administration, Silver Spring, Maryland, USA.
Bin ZhouCDC COVID-19 Response, Centers for Disease Control and Prevention, Atlanta, Georgia, USA.
Charles T DavisCDC COVID-19 Response, Centers for Disease Control and Prevention, Atlanta, Georgia, USA.
David E WentworthCDC COVID-19 Response, Centers for Disease Control and Prevention, Atlanta, Georgia, USA.
Wilbur H ChenCenter for Vaccine Development and Global Health, University of Maryland School of Medicine, Baltimore, Maryland, USA.
Mallory C ShriverCenter for Vaccine Development and Global Health, University of Maryland School of Medicine, Baltimore, Maryland, USA.
Robin S BarnesCenter for Vaccine Development and Global Health, University of Maryland School of Medicine, Baltimore, Maryland, USA.
Marcela F PasettiCenter for Vaccine Development and Global Health, University of Maryland School of Medicine, Baltimore, Maryland, USA.
Jerry P WeirLaboratory of DNA viruses, Division of Viral Products, Center for Biologics Evaluation and Research, Office of Vaccines Research and Review, United States Food and Drug Administration, Silver Spring, Maryland, USA.
Bing ChenDivision of Molecular Medicine, Boston Children's Hospital, Boston, Massachusetts, USA.
Hang XieLaboratory of Pediatric and Respiratory Viral Diseases, Division of Viral Products, Center for Biologics Evaluation and Research, Office of Vaccines Research and Review, United States Food and Drug Administration, Silver Spring, Maryland, USA.ORCID 0000-0001-8318-5554

Funding

Structure-function studies of the membrane-interacting domains of HIV-1 Env spikeR01AI127193 · NIAID · BOSTON CHILDREN'S HOSPITAL · PI CHEN, BING, HARRISON, STEPHEN COPLAN · 2016 to 2025
$8.4M
Structure of the full-length spike protein of SARS-CoV-2 in the context of membraneR01AI147884 · NIAID · BOSTON CHILDREN'S HOSPITAL · PI CHEN, BING · 2020 to 2024
$3.4M
Intramural FDA HHS FD999999NIAID NIH HHS R01 AI127193NIAID NIH HHS R01 AI147884
6 · The paper itself

Abstract

Broadly neutralizing antibodies against severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) variants are sought to curb coronavirus disease 2019 (COVID-19) infections. Here we produced and characterized a set of mouse monoclonal antibodies (mAbs) specific for the ancestral SARS-CoV-2 receptor binding domain (RBD). Two of them, 17A7 and 17B10, were highly potent in microneutralization assay with 50% inhibitory concentration (IC

Indexed as

Antibodies, MonoclonalCOVID-19AnimalsAntibodies, NeutralizingAntibodies, ViralCOVID-19 SerotherapyHumansMiceMice, TransgenicNeutralization TestsSARS-CoV-2Spike Glycoprotein, CoronavirusAntibodies, MonoclonalAntibodies, NeutralizingAntibodies, ViralSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2cross-neutralizationneutralizing antibodyRBD-reactive antibodyreceptor binding domain (RBD)SARS-CoV-2structural analysis

Identifiers

PMID36916782
PMCPMC10189799

What OpenQuestion holds

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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.