Evidence map›Paper›PMID 33139569›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2020

Rapid identification of a human antibody with high prophylactic and therapeutic efficacy in three animal models of SARS-CoV-2 infection.

Wei Li, Chuan Chen, Aleksandra Drelich, David R Martinez, Lisa E Gralinski, Zehua Sun, Alexandra Schäfer, Swarali S Kulkarni, Xianglei Liu, Sarah R Leist and 10 more

Open access · hybridAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed, 1 pooled it
2.1field-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

65 citing papers in PubMed, 1 synthesis or guideline pooled it, 92 citations in OpenAlex.

  1. Prophylaxis for COVID-19: a systematic review.Clinical microbiology and infection : the official publication of the European Society of Clinical Microbiology and Infectious Diseases · 2021
    Pooled it
  2. Trial
  3. Article
  4. Article
  5. Technologies for Monoclonal Antibody Discovery and Development.International journal of molecular sciences · 2025
    Review
  6. Article
  7. Antibody-dependent enhancement of coronaviruses.International journal of biological sciences · 2025
    Review
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5 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

20 authors at 4 institutions in 2 countries.

Wei LiDepartment of Medicine, Division of Infectious Diseases, Center for Antibody Therapeutics, University of Pittsburgh Medical School, Pittsburgh, PA 15261; LIWEI171@pitt.edu mit666666@pitt.edu.ORCID 0000-0002-6960-7404
Chuan ChenDepartment of Medicine, Division of Infectious Diseases, Center for Antibody Therapeutics, University of Pittsburgh Medical School, Pittsburgh, PA 15261.
Aleksandra DrelichDepartment of Microbiology and Immunology, Centers for Biodefense and Emerging Diseases, Galveston National Laboratory, Galveston, TX 77550.ORCID 0000-0002-0201-5017
David R MartinezDepartment of Epidemiology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599.
Lisa E GralinskiDepartment of Epidemiology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599.ORCID 0000-0003-1374-8002
Zehua SunDepartment of Medicine, Division of Infectious Diseases, Center for Antibody Therapeutics, University of Pittsburgh Medical School, Pittsburgh, PA 15261.ORCID 0000-0003-4287-1763
Alexandra SchäferDepartment of Epidemiology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599.
Swarali S KulkarniDepartment of Veterinary Microbiology, Vaccine and Infectious Disease Organization-International Vaccine Centre, University of Saskatchewan, Saskatoon, SK S7N 5E3, Canada.ORCID 0000-0002-2595-5968
Xianglei LiuDepartment of Medicine, Division of Infectious Diseases, Center for Antibody Therapeutics, University of Pittsburgh Medical School, Pittsburgh, PA 15261.
Sarah R LeistDepartment of Epidemiology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599.ORCID 0000-0002-4989-5381
Doncho V ZhelevDepartment of Medicine, Division of Infectious Diseases, Center for Antibody Therapeutics, University of Pittsburgh Medical School, Pittsburgh, PA 15261.ORCID 0000-0001-8800-7044
Liyong ZhangDepartment of Medicine, Division of Infectious Diseases, Center for Antibody Therapeutics, University of Pittsburgh Medical School, Pittsburgh, PA 15261.ORCID 0000-0002-6952-7463
Ye-Jin KimDepartment of Medicine, Division of Infectious Diseases, Center for Antibody Therapeutics, University of Pittsburgh Medical School, Pittsburgh, PA 15261.ORCID 0000-0003-2150-9378
Eric C PetersonAbound Bio, Pittsburgh, PA 15219.
Alex ConardAbound Bio, Pittsburgh, PA 15219.ORCID 0000-0003-0856-134X
John W MellorsDepartment of Medicine, Division of Infectious Diseases, Center for Antibody Therapeutics, University of Pittsburgh Medical School, Pittsburgh, PA 15261.
Chien-Te K TsengDepartment of Microbiology and Immunology, Centers for Biodefense and Emerging Diseases, Galveston National Laboratory, Galveston, TX 77550.ORCID 0000-0001-5726-9834
Darryl FalzaranoDepartment of Veterinary Microbiology, Vaccine and Infectious Disease Organization-International Vaccine Centre, University of Saskatchewan, Saskatoon, SK S7N 5E3, Canada.ORCID 0000-0002-8805-8068
Ralph S BaricDepartment of Epidemiology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599.
Dimiter S DimitrovDepartment of Medicine, Division of Infectious Diseases, Center for Antibody Therapeutics, University of Pittsburgh Medical School, Pittsburgh, PA 15261; LIWEI171@pitt.edu mit666666@pitt.edu.ORCID 0000-0002-2258-1024
University of Pittsburgh · USUniversity of North Carolina at Chapel Hill · USAbound Bio (United States) · USUniversity of Saskatchewan · CA

Funding

Virology Research Program (Program 4)P30CA016086 · NCI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI Deborah F. Tate · 1985 to 2026
$201.5M
Broad-spectrum antiviral GS-5734 to treat MERS-CoV and related emerging CoVR01AI132178 · NIAID · UNIV OF NORTH CAROLINA CHAPEL HILL · PI BARIC, RALPH S, SHEAHAN, TIMOTHY PATRICK · 2017 to 2021
$7.0M
Determinants of Coronavirus Fidelity in Replication and PathogenesisR01AI108197 · NIAID · VANDERBILT UNIVERSITY MEDICAL CENTER · PI BARIC, RALPH S, DENISON, MARK R · 2013 to 2022
$6.5M
Human antibody-based countermeasures against the Wuhan Coronavirus SARS-CoV-2R01AI157155 · NIAID · WASHINGTON UNIVERSITY · PI BARIC, RALPH S, CROWE, JAMES E · 2020 to 2024
$6.0M
INFECTIOUS DISEASE PATHOGENESIS TRAININGT32AI007151 · NIAID · UNIV OF NORTH CAROLINA CHAPEL HILL · PI JULIANO, JONATHAN J · 1985 to 2024
$5.5M
Defining viral and immune mechanisms of Dengue virus serotype 2 immune evasionF32AI152296 · NIAID · UNIV OF NORTH CAROLINA CHAPEL HILL · PI MARTINEZ, DAVID R. · 2020 to 2020
$41k
NCI NIH HHS P30 CA016086NIAID NIH HHS F32 AI152296NIAID NIH HHS R01 AI108197NIAID NIH HHS R01 AI132178NIAID NIH HHS R01 AI157155NIAID NIH HHS T32 AI007151NIH HHS AI 108197NIH HHS AI132178Wellcome Trust
6 · The paper itself

Abstract

Effective therapies are urgently needed for the SARS-CoV-2/COVID-19 pandemic. We identified panels of fully human monoclonal antibodies (mAbs) from large phage-displayed Fab, scFv, and VH libraries by panning against the receptor binding domain (RBD) of the SARS-CoV-2 spike (S) glycoprotein. A high-affinity Fab was selected from one of the libraries and converted to a full-size antibody, IgG1 ab1, which competed with human ACE2 for binding to RBD. It potently neutralized replication-competent SARS-CoV-2 but not SARS-CoV, as measured by two different tissue culture assays, as well as a replication-competent mouse ACE2-adapted SARS-CoV-2 in BALB/c mice and native virus in hACE2-expressing transgenic mice showing activity at the lowest tested dose of 2 mg/kg. IgG1 ab1 also exhibited high prophylactic and therapeutic efficacy in a hamster model of SARS-CoV-2 infection. The mechanism of neutralization is by competition with ACE2 but could involve antibody-dependent cellular cytotoxicity (ADCC) as IgG1 ab1 had ADCC activity in vitro. The ab1 sequence has a relatively low number of somatic mutations, indicating that ab1-like antibodies could be quickly elicited during natural SARS-CoV-2 infection or by RBD-based vaccines. IgG1 ab1 did not aggregate, did not exhibit other developability liabilities, and did not bind to any of the 5,300 human membrane-associated proteins tested. These results suggest that IgG1 ab1 has potential for therapy and prophylaxis of SARS-CoV-2 infections. The rapid identification (within 6 d of availability of antigen for panning) of potent mAbs shows the value of large antibody libraries for response to public health threats from emerging microbes.

Indexed as

Angiotensin-Converting Enzyme 2AnimalsAntibodies, ViralAntibody-Dependent Cell CytotoxicityChlorocebus aethiopsCOVID-19COVID-19 Serological TestingCOVID-19 SerotherapyCOVID-19 VaccinesCricetinaeFemaleHumansImmunization, PassiveImmunogenicity, VaccineImmunoglobulin GMiceAngiotensin-Converting Enzyme 2Antibodies, ViralCOVID-19 VaccinesImmunoglobulin GSpike Glycoprotein, Coronavirusspike protein, SARS-CoV-2animal modelscoronavirusesSARS-CoV-2therapeutic antibodies

Identifiers

PMID33139569
PMCPMC7703590
OpenAlexW3095090886

What Socratic 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 Socratic graph.