Evidence map›Paper›PMID 32320678›Full record

ArticleCell host & microbe2020

Non-neutralizing Antibodies from a Marburg Infection Survivor Mediate Protection by Fc-Effector Functions and by Enhancing Efficacy of Other Antibodies.

Philipp A Ilinykh, Kai Huang, Rodrigo I Santos, Pavlo Gilchuk, Bronwyn M Gunn, Marcus M Karim, Jenny Liang, Mallorie E Fouch, Edgar Davidson, Diptiben V Parekh and 9 more

Abstract read
In one paragraph

Article in Cell host & microbe, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed, 1 pooled it
–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

57 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Mucosal immune response in biology, disease prevention and treatment.Signal transduction and targeted therapy · 2025
    Pooled it
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

19 authors.

Philipp A IlinykhDepartment of Pathology, University of Texas Medical Branch, Galveston, TX, USA; Galveston National Laboratory, Galveston, TX, USA.
Kai HuangDepartment of Pathology, University of Texas Medical Branch, Galveston, TX, USA; Galveston National Laboratory, Galveston, TX, USA.
Rodrigo I SantosDepartment of Pathology, University of Texas Medical Branch, Galveston, TX, USA; Galveston National Laboratory, Galveston, TX, USA.
Pavlo GilchukVanderbilt Vaccine Center, Vanderbilt University Medical Center, Nashville, TN, USA.
Bronwyn M GunnRagon Institute of MGH, MIT, and Harvard, Cambridge, MA, USA.
Marcus M KarimRagon Institute of MGH, MIT, and Harvard, Cambridge, MA, USA.
Jenny LiangIntegral Molecular, Philadelphia, PA 19104, USA.
Mallorie E FouchIntegral Molecular, Philadelphia, PA 19104, USA.
Edgar DavidsonIntegral Molecular, Philadelphia, PA 19104, USA.
Diptiben V ParekhDepartment of Immunology and Microbiology, The Scripps Research Institute, La Jolla, CA, USA.
James B KimbleDepartment of Pathology, University of Texas Medical Branch, Galveston, TX, USA; Galveston National Laboratory, Galveston, TX, USA.
Colette A PietzschDepartment of Pathology, University of Texas Medical Branch, Galveston, TX, USA; Galveston National Laboratory, Galveston, TX, USA.
Michelle MeyerDepartment of Pathology, University of Texas Medical Branch, Galveston, TX, USA; Galveston National Laboratory, Galveston, TX, USA.
Natalia A KuzminaDepartment of Pathology, University of Texas Medical Branch, Galveston, TX, USA; Galveston National Laboratory, Galveston, TX, USA.
Larry ZeitlinMapp Biopharmaceutical, San Diego, CA, USA.
Erica Ollmann SaphireDepartment of Immunology and Microbiology, The Scripps Research Institute, La Jolla, CA, USA; Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA, USA.
Galit AlterRagon Institute of MGH, MIT, and Harvard, Cambridge, MA, USA.
James E CroweVanderbilt Vaccine Center, Vanderbilt University Medical Center, Nashville, TN, USA; Department of Pathology, Microbiology, and Immunology, Vanderbilt University Medical Center, Nashville, TN, USA; Department of Pediatrics (Infectious Diseases), Vanderbilt University Medical Center, Nashville, TN, USA. Electronic address: james.crowe@vumc.org.
Alexander BukreyevDepartment of Pathology, University of Texas Medical Branch, Galveston, TX, USA; Department of Microbiology and Immunology, University of Texas Medical Branch, Galveston, TX; Galveston National Laboratory, Galveston, TX, USA. Electronic address: alexander.bukreyev@utmb.edu.

Funding

Specific and Broadly Active Monoclonal Antibody Therapeutics Against The FilovirusesU19AI142790 · NIAID · LA JOLLA INSTITUTE FOR IMMUNOLOGY · PI SAPHIRE, ERICA OLLMANN · 2019 to 2023
$40.0M
Research Project 3: siRNA Therapy and Small Molecule Combination Treatment for FilovirusesU19AI142785 · NIAID · UNIVERSITY OF TEXAS MED BR GALVESTON · PI GEISBERT, THOMAS WILLIAM · 2019 to 2023
$35.5M
Supplemental Research Project (SRP)U19AI109711 · NIAID · UNIVERSITY OF TEXAS MED BR GALVESTON · PI GEISBERT, THOMAS WILLIAM · 2014 to 2018
$26.6M
B-Cell Epitope Discovery and Mechanisms of Antibody Protection for ZIKV, MARV, VEEV Envelope Proteins 75N93019C00073 · NIAID · INTEGRAL MOLECULAR · PI DORANZ, BENJAMIN · 2019 to 2023
$7.5M
NIAID NIH HHS 75N93019C00073NIAID NIH HHS U19 AI109711NIAID NIH HHS U19 AI142785NIAID NIH HHS U19 AI142790
6 · The paper itself

Abstract

Marburg virus (MARV) and Ebola virus (EBOV) belong to the family Filoviridae. MARV causes severe disease in humans with high fatality. We previously isolated a large panel of monoclonal antibodies (mAbs) from B cells of a human survivor with previous naturally acquired MARV infection. Here, we characterized functional properties of these mAbs and identified non-neutralizing mAbs targeting the glycoprotein (GP) 2 portion of the mucin-like domain (MLD) of MARV GP, termed the wing region. One mAb targeting the GP2 wing, MR228, showed therapeutic protection in mice and guinea pigs infected with MARV. The protection was mediated by the Fc fragment functions of MR228. Binding of another GP2 wing-specific non-neutralizing mAb, MR235, to MARV GP increased accessibility of epitopes in the receptor-binding site (RBS) for neutralizing mAbs, resulting in enhanced virus neutralization by these mAbs. These findings highlight an important role for non-neutralizing mAbs during natural human MARV infection.

Indexed as

AnimalsAntibodies, MonoclonalAntibodies, NeutralizingAntibodies, ViralB-LymphocytesChlorocebus aethiopsDisease Models, AnimalEbolavirusEpitopesFemaleGlycoproteinsGuinea PigsHEK293 CellsHumansMaleMarburgvirusAntibodies, MonoclonalAntibodies, NeutralizingAntibodies, ViralEpitopesGlycoproteinsViral Envelope Proteinsanimal models of filovirus infectionantibodiescooperativity of antibody bindingFc-mediated protective effectsglycoproteinMarburg virus

Identifiers

PMID32320678
PMCPMC7292764

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Registered trials

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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.