Evidence map›Paper›PMID 32783883›Full record

ArticleCell host & microbe2020

Human mAbs Broadly Protect against Arthritogenic Alphaviruses by Recognizing Conserved Elements of the Mxra8 Receptor-Binding Site.

Laura A Powell, Andrew Miller, Julie M Fox, Nurgun Kose, Thomas Klose, Arthur S Kim, Robin Bombardi, Rashika N Tennekoon, A Dharshan de Silva, Robert H Carnahan and 4 more

Open access · bronzeAbstract 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 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
6.0field-weighted citation impact, top 3% 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

49 citing papers in PubMed, 63 citations in OpenAlex.

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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

14 authors at 5 institutions in 2 countries.

Laura A PowellDepartment of Pathology, Microbiology and Immunology, Vanderbilt University Medical Center, Nashville, TN 37232, USA.
Andrew MillerDepartment of Biological Sciences, Purdue University, West Lafayette, IN 47907, USA.
Julie M FoxDepartment of Medicine, Washington University School of Medicine, Saint Louis, MO 63110, USA.
Nurgun KoseVanderbilt Vaccine Center, Department of Pediatrics, Nashville, TN 37232, USA.
Thomas KloseDepartment of Biological Sciences, Purdue University, West Lafayette, IN 47907, USA.
Arthur S KimDepartment of Medicine, Washington University School of Medicine, Saint Louis, MO 63110, USA; Department of Pathology and Immunology, Washington University School of Medicine, Saint Louis, MO 63110, USA.
Robin BombardiVanderbilt Vaccine Center, Department of Pediatrics, Nashville, TN 37232, USA.
Rashika N TennekoonGenetech Research Institute, Colombo, Sri Lanka; Department of Paraclinical Sciences, Faculty of Medicine, Kotelawala Defence University, Colombo, Sri Lanka.
A Dharshan de SilvaGenetech Research Institute, Colombo, Sri Lanka; Department of Paraclinical Sciences, Faculty of Medicine, Kotelawala Defence University, Colombo, Sri Lanka.
Robert H CarnahanVanderbilt Vaccine Center, Department of Pediatrics, Nashville, TN 37232, USA; Department of Pediatrics, Vanderbilt University Medical Center, Nashville, TN 37232, USA.
Michael S DiamondDepartment of Molecular Microbiology, Washington University School of Medicine, Saint Louis, MO 63110, USA; Department of Medicine, Washington University School of Medicine, Saint Louis, MO 63110, USA; Department of Pathology and Immunology, Washington University School of Medicine, Saint Louis, MO 63110, USA; Andrew M. and Jane M. Bursky Center for Human Immunology and Immunotherapy Programs, Washington University School of Medicine, Saint Louis, MO 63110, USA.
Michael G RossmannDepartment of Biological Sciences, Purdue University, West Lafayette, IN 47907, USA.
Richard J KuhnDepartment of Biological Sciences, Purdue University, West Lafayette, IN 47907, USA; Markey Center for Structural Biology and Purdue Institute of Inflammation, Immunology and Infectious Disease, Purdue University, West Lafayette, IN 47907, USA.
James E CroweDepartment of Pathology, Microbiology and Immunology, Vanderbilt University Medical Center, Nashville, TN 37232, USA; Vanderbilt Vaccine Center, Department of Pediatrics, Nashville, TN 37232, USA; Department of Pediatrics, Vanderbilt University Medical Center, Nashville, TN 37232, USA. Electronic address: james.crowe@vumc.org.
Purdue University West Lafayette · USVanderbilt University · USWashington University in St. Louis · USGeneral Sir John Kotelawala Defence University · LKVanderbilt University Medical Center · US

Funding

Specific and Broadly Active Monoclonal Antibody Therapeutics Against The FilovirusesU19AI142790 · NIAID · LA JOLLA INSTITUTE FOR IMMUNOLOGY · PI DIAMOND, MICHAEL S · 2019 to 2023
$40.0M
Structural Studies of TogavirusesR01AI095366 · NIAID · PURDUE UNIVERSITY · PI KUHN, RICHARD J. · 2012 to 2023
$6.8M
Structure-Function Analysis of Mxra8 Interaction with Alphaviruses.R01AI143673 · NIAID · WASHINGTON UNIVERSITY · PI DIAMOND, MICHAEL S, FREMONT, DAVED H. · 2019 to 2025
$6.5M
Structural and functional basis of ultra potent CHKV neutralization by human mAbsR01AI114816 · NIAID · VANDERBILT UNIVERSITY MEDICAL CENTER · PI CROWE, JAMES E, DIAMOND, MICHAEL S · 2015 to 2019
$3.7M
NIAID NIH HHS HHSN272201400018CNIAID NIH HHS R01 AI095366NIAID NIH HHS R01 AI114816NIAID NIH HHS R01 AI143673NIAID NIH HHS U19 AI142790
6 · The paper itself

Abstract

Mosquito inoculation of humans with arthritogenic alphaviruses results in a febrile syndrome characterized by debilitating musculoskeletal pain and arthritis. Despite an expanding global disease burden, no approved therapies or licensed vaccines exist. Here, we describe human monoclonal antibodies (mAbs) that bind to and neutralize multiple distantly related alphaviruses. These mAbs compete for an antigenic site and prevent attachment to the recently discovered Mxra8 alphavirus receptor. Three cryoelectron microscopy structures of Fab in complex with Ross River (RRV), Mayaro, or chikungunya viruses reveal a conserved footprint of the broadly neutralizing mAb RRV-12 in a region of the E2 glycoprotein B domain. This mAb neutralizes virus in vitro by preventing virus entry and spread and is protective in vivo in mouse models. Thus, the RRV-12 mAb and its defined epitope have potential as a therapeutic agent or target of vaccine design against multiple emerging arthritogenic alphavirus infections.

Indexed as

Binding SitesAlphavirusAlphavirus InfectionsAnimalsAntibodies, MonoclonalAntibodies, NeutralizingAntibodies, ViralArthritisChikungunya virusChlorocebus aethiopsCross ReactionsCryoelectron MicroscopyEpitopesFemaleHumansImmunoglobulinsalphavirus receptorAntibodies, MonoclonalAntibodies, NeutralizingAntibodies, ViralEpitopesImmunoglobulinsMembrane ProteinsMxra8 protein, mouseReceptors, VirusalphavirusantibodiesarthritisChikungunya viruscross-reactivityinfectiousMayaro virusO’nyong’nyong virusRoss River virusviral

Identifiers

PMID32783883
PMCPMC7666055
OpenAlexW3048369683

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.