Evidence map›Paper›PMID 32826914›Full record

ArticleNature communications2020

A cross-reactive human IgA monoclonal antibody blocks SARS-CoV-2 spike-ACE2 interaction.

Monir Ejemel, Qi Li, Shurong Hou, Zachary A Schiller, Julia A Tree, Aaron Wallace, Alla Amcheslavsky, Nese Kurt Yilmaz, Karen R Buttigieg, Michael J Elmore and 15 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 109 papers.

0numbers the graph read from it
0cells of the map it votes in
109citing papers in PubMed
3.6field-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

109 citing papers in PubMed, 177 citations in OpenAlex.

  1. Review
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  5. Materials today. Bio · 2026
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  17. Stability Engineering of Recombinant Secretory IgA.International journal of molecular sciences · 2024
    Article
  18. Review
  19. Article
  20. Article

49 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

25 authors at 3 institutions in 2 countries.

Monir Ejemel *MassBiologics of the University of Massachusetts Medical School, Boston, MA, USA.
Qi Li *MassBiologics of the University of Massachusetts Medical School, Boston, MA, USA.
Shurong Hou *Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Boston, MA, USA.ORCID http://orcid.org/0000-0001-5143-0797
Zachary A Schiller *MassBiologics of the University of Massachusetts Medical School, Boston, MA, USA.ORCID http://orcid.org/0000-0002-4185-2416
Julia A TreeNational Infection Service, Public Health England, Porton Down, Salisbury, Wiltshire, UK.
Aaron WallaceMassBiologics of the University of Massachusetts Medical School, Boston, MA, USA.
Alla AmcheslavskyMassBiologics of the University of Massachusetts Medical School, Boston, MA, USA.
Nese Kurt YilmazBiochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Boston, MA, USA.
Karen R ButtigiegNational Infection Service, Public Health England, Porton Down, Salisbury, Wiltshire, UK.
Michael J ElmoreNational Infection Service, Public Health England, Porton Down, Salisbury, Wiltshire, UK.ORCID http://orcid.org/0000-0001-9425-2660
Kerry GodwinNational Infection Service, Public Health England, Porton Down, Salisbury, Wiltshire, UK.
Naomi CoombesNational Infection Service, Public Health England, Porton Down, Salisbury, Wiltshire, UK.
Jacqueline R ToomeyMassBiologics of the University of Massachusetts Medical School, Boston, MA, USA.
Ryan SchneiderMassBiologics of the University of Massachusetts Medical School, Boston, MA, USA.
Anudeep S RamchettyMassBiologics of the University of Massachusetts Medical School, Boston, MA, USA.
Brianna J CloseNational Emerging Infectious Diseases Laboratories, Boston University, Boston, MA, USA.ORCID http://orcid.org/0000-0002-0563-1464
Da-Yuan ChenNational Emerging Infectious Diseases Laboratories, Boston University, Boston, MA, USA.
Hasahn L ConwayNational Emerging Infectious Diseases Laboratories, Boston University, Boston, MA, USA.ORCID http://orcid.org/0000-0001-7328-3521
Mohsan SaeedNational Emerging Infectious Diseases Laboratories, Boston University, Boston, MA, USA.
Chandrashekar GanesaMassBiologics of the University of Massachusetts Medical School, Boston, MA, USA.
Miles W CarrollNational Infection Service, Public Health England, Porton Down, Salisbury, Wiltshire, UK.
Lisa A CavaciniMassBiologics of the University of Massachusetts Medical School, Boston, MA, USA. Lisa.Cavacini@umassmed.edu.ORCID http://orcid.org/0000-0003-1417-8339
Mark S KlempnerMassBiologics of the University of Massachusetts Medical School, Boston, MA, USA. Mark.Klempner@umassmed.edu.
Celia A SchifferBiochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Boston, MA, USA. Celia.Schiffer@umassmed.edu.ORCID http://orcid.org/0000-0003-2270-6613
Yang WangMassBiologics of the University of Massachusetts Medical School, Boston, MA, USA. Yang.Wang@umassmed.edu.ORCID http://orcid.org/0000-0002-5554-8247
University of Massachusetts Chan Medical School · USPublic Health England · GBBoston University · US

Funding

Nonhuman Primate Reagent ResourceU24AI126683 · NIAID · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI Diogo Magnani · 2016 to 2026
$20.1M
Structurally dissecting APOBEC3's for HIV-1 restriction and beyondR01AI150478 · NIAID · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI SCHIFFER, CELIA A. · 2019 to 2024
$3.9M
VACCINE PRODUCTION FACILITYN01AI065315 · NIAID · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI AMBROSINO, DONNA M · 1996 to 2000
$1.0M
NIAID NIH HHS N01 AI065315NIAID NIH HHS R01 AI150478NIAID NIH HHS U24 AI126683
6 · The paper itself

Abstract

COVID-19 caused by SARS-CoV-2 has become a global pandemic requiring the development of interventions for the prevention or treatment to curtail mortality and morbidity. No vaccine to boost mucosal immunity, or as a therapeutic, has yet been developed to SARS-CoV-2. In this study, we discover and characterize a cross-reactive human IgA monoclonal antibody, MAb362. MAb362 binds to both SARS-CoV and SARS-CoV-2 spike proteins and competitively blocks ACE2 receptor binding, by overlapping the ACE2 structural binding epitope. Furthermore, MAb362 IgA neutralizes both pseudotyped SARS-CoV and SARS-CoV-2 in 293 cells expressing ACE2. When converted to secretory IgA, MAb326 also neutralizes authentic SARS-CoV-2 virus while the IgG isotype shows no neutralization. Our results suggest that SARS-CoV-2 specific IgA antibodies, such as MAb362, may provide effective immunity against SARS-CoV-2 by inducing mucosal immunity within the respiratory system, a potentially critical feature of an effective vaccine.

Indexed as

Angiotensin-Converting Enzyme 2AnimalsAntibodies, MonoclonalAntibodies, NeutralizingBetacoronavirusChlorocebus aethiopsCross ReactionsEpitopesHEK293 CellsHumansImmunoglobulin AImmunoglobulin A, SecretoryImmunoglobulin GModels, MolecularMutationPeptidyl-Dipeptidase AACE2 protein, humanAngiotensin-Converting Enzyme 2Antibodies, MonoclonalAntibodies, NeutralizingEpitopesImmunoglobulin AImmunoglobulin A, SecretoryImmunoglobulin GPeptidyl-Dipeptidase ASpike Glycoprotein, Coronavirus

Identifiers

PMID32826914
PMCPMC7442812
OpenAlexW3080999659

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.