Evidence map›Paper›PMID 33782133›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2021

Potent neutralization of Rift Valley fever virus by human monoclonal antibodies through fusion inhibition.

Nathaniel S Chapman, Haiyan Zhao, Nurgun Kose, Jonna B Westover, Birte Kalveram, Robin Bombardi, Jessica Rodriguez, Rachel Sutton, Joseph Genualdi, A Desiree LaBeaud and 6 more

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
1.9field-weighted citation impact, top 12% 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

32 citing papers in PubMed, 36 citations in OpenAlex.

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  7. Cryo-EM structure of the Rift Valley fever virus envelope protein in complex with a potent neutralization antibody.Proceedings of the National Academy of Sciences of the United States of America · 2025
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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

16 authors at 7 institutions in 2 countries.

Nathaniel S ChapmanDepartment of Pathology, Microbiology and Immunology, Vanderbilt University Medical Center, Nashville, TN 37232.
Haiyan ZhaoDepartment of Pathology and Immunology, Washington University School of Medicine, St. Louis, MO 63110.ORCID 0000-0001-5123-5537
Nurgun KoseThe Vanderbilt Vaccine Center, Vanderbilt University Medical Center, Nashville, TN 37232.
Jonna B WestoverDepartment of Animal, Dairy, and Veterinary Sciences, Utah State University, Logan, UT 84322.
Birte KalveramDepartment of Pathology, The University of Texas Medical Branch at Galveston, Galveston, TX 77555.
Robin BombardiThe Vanderbilt Vaccine Center, Vanderbilt University Medical Center, Nashville, TN 37232.
Jessica RodriguezThe Vanderbilt Vaccine Center, Vanderbilt University Medical Center, Nashville, TN 37232.
Rachel SuttonThe Vanderbilt Vaccine Center, Vanderbilt University Medical Center, Nashville, TN 37232.
Joseph GenualdiThe Vanderbilt Vaccine Center, Vanderbilt University Medical Center, Nashville, TN 37232.
A Desiree LaBeaudDepartment of Pediatrics, Division of Infectious Diseases, Stanford University School of Medicine, Stanford, CA 94305.ORCID 0000-0001-8364-6867
Francis M MutukuDepartment of Environment and Health Sciences, Technical University of Mombasa, Mombasa, Kenya.ORCID 0000-0002-9000-7008
Phillip R PittmanMedical Research and Material Command, U.S. Army Medical Research Institute of Infectious Diseases, Fort Detrick, MD 21702.ORCID 0000-0003-1787-759X
Alexander N FreibergDepartment of Pathology, The University of Texas Medical Branch at Galveston, Galveston, TX 77555.ORCID 0000-0001-8413-8960
Brian B GowenDepartment of Animal, Dairy, and Veterinary Sciences, Utah State University, Logan, UT 84322.ORCID 0000-0001-9113-2575
Daved H FremontDepartment of Pathology and Immunology, Washington University School of Medicine, St. Louis, MO 63110.ORCID 0000-0002-8544-2689
James E CroweDepartment of Pathology, Microbiology and Immunology, Vanderbilt University Medical Center, Nashville, TN 37232; james.crowe@vumc.org.ORCID 0000-0002-0049-1079
Vanderbilt University Medical Center · USThe University of Texas Medical Branch at Galveston · USUtah State University · USWashington University in St. Louis · USStanford University · USTechnical University of Mombasa · KEUnited States Army Medical Research Institute of Infectious Diseases · US

Funding

COVID Supplement B Cell Epitope Discovery and Mechanisms of Antibody Protection.75N93019C00062 · NIAID · WASHINGTON UNIVERSITY · PI FREMONT, DAVED · 2019 to 2023
$11.7M
Eco-epidemiology of Schistosomiasis, Malaria and Polyparasitism in Coastal KenyaR01TW008067 · FIC · CASE WESTERN RESERVE UNIVERSITY · PI KING, CHARLES HARDING, KITRON, URIEL DAN · 2007 to 2011
$2.4M
Integrated automated liquid handling system for novel antibody discoveryS10OD021737 · OD · VANDERBILT UNIVERSITY · PI CARNAHAN, ROBERT H · 2016 to 2016
$1.2M
FIC NIH HHS R01 TW008067NIAID NIH HHS 75N93019C00062NIAID NIH HHS HHSN272201700041INIH HHS S10 OD021737
6 · The paper itself

Abstract

Rift Valley fever virus (RVFV), an emerging arboviral and zoonotic bunyavirus, causes severe disease in livestock and humans. Here, we report the isolation of a panel of monoclonal antibodies (mAbs) from the B cells of immune individuals following natural infection in Kenya or immunization with MP-12 vaccine. The B cell responses of individuals who were vaccinated or naturally infected recognized similar epitopes on both Gc and Gn proteins. The Gn-specific mAbs and two mAbs that do not recognize either monomeric Gc or Gn alone but recognized the hetero-oligomer glycoprotein complex (Gc+Gn) when Gc and Gn were coexpressed exhibited potent neutralizing activities in vitro, while Gc-specific mAbs exhibited relatively lower neutralizing capacity. The two Gc+Gn-specific mAbs and the Gn domain A-specific mAbs inhibited RVFV fusion to cells, suggesting that mAbs can inhibit the exposure of the fusion loop in Gc, a class II fusion protein, and thus prevent fusion by an indirect mechanism without direct fusion loop contact. Competition-binding analysis with coexpressed Gc/Gn and mutagenesis library screening indicated that these mAbs recognize four major antigenic sites, with two sites of vulnerability for neutralization on Gn. In experimental models of infection in mice, representative mAbs recognizing three of the antigenic sites reduced morbidity and mortality when used at a low dose in both prophylactic and therapeutic settings. This study identifies multiple candidate mAbs that may be suitable for use in humans against RVFV infection and highlights fusion inhibition against bunyaviruses as a potential contributor to potent antibody-mediated neutralization.

Indexed as

AnimalsAntibodies, MonoclonalAntibodies, NeutralizingAntibodies, ViralCell Line, TumorCells, CulturedChlorocebus aethiopsEpitopesHEK293 CellsHumansMiceMice, Inbred C57BLRift Valley fever virusVero CellsViral Fusion ProteinsAntibodies, MonoclonalAntibodies, NeutralizingAntibodies, ViralEpitopesViral Fusion Proteinsadaptive immunityantibodiesmonoclonalPhlebovirusRift Valley fever virusvirus internalization

Identifiers

PMID33782133
PMCPMC8040655
OpenAlexW3139697227

What OpenQuestion holds

Textmetadata
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.