Evidence map›Paper›PMID 32938765›Full record

ArticleJournal of virology2020

Reovirus σ1 Conformational Flexibility Modulates the Efficiency of Host Cell Attachment.

Julia R Diller, Sean R Halloran, Melanie Koehler, Rita Dos Santos Natividade, David Alsteens, Thilo Stehle, Terence S Dermody, Kristen M Ogden

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.0field-weighted citation impact, top 20% 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

13 citing papers in PubMed, 19 citations in OpenAlex.

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  11. Deciphering molecular mechanisms stabilizing the reovirus-binding complex.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
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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

8 authors at 5 institutions in 3 countries.

Julia R DillerDepartment of Pediatrics, Vanderbilt University Medical Center, Nashville, Tennessee, USA.
Sean R HalloranDepartment of Pediatrics, Vanderbilt University Medical Center, Nashville, Tennessee, USA.
Melanie KoehlerLouvain Institute of Biomolecular Science and Technology, Université Catholique de Louvain, Ottignies-Louvain-la-Neuve, Belgium.ORCID 0000-0003-3042-1749
Rita Dos Santos NatividadeLouvain Institute of Biomolecular Science and Technology, Université Catholique de Louvain, Ottignies-Louvain-la-Neuve, Belgium.
David AlsteensLouvain Institute of Biomolecular Science and Technology, Université Catholique de Louvain, Ottignies-Louvain-la-Neuve, Belgium.ORCID 0000-0001-9229-113X
Thilo StehleInterfaculty Institute of Biochemistry, University of Tübingen, Tübingen, Germany.ORCID 0000-0002-4571-8548
Terence S DermodyDepartments of Pediatrics and Microbiology and Molecular Genetics, University of Pittsburgh School of Medicine, and Center for Microbial Pathogenesis, UPMC Children's Hospital of Pittsburgh, Pittsburgh, Pennsylvania, USA terence.dermody@chp.edu kristen.ogden@vumc.org.ORCID 0000-0003-1853-8741
Kristen M OgdenDepartment of Pediatrics, Vanderbilt University Medical Center, Nashville, Tennessee, USA terence.dermody@chp.edu kristen.ogden@vumc.org.ORCID 0000-0002-2670-4335
Vanderbilt University Medical Center · USUCLouvain · BEUniversity of Pittsburgh · USUniversity of Tübingen · DEWalloon Excellence in Lifesciences and Biotechnology · BE

Funding

Translational Analysis CoreP30DK058404 · NIDDK · VANDERBILT UNIVERSITY MEDICAL CENTER · PI RICHARD M. PEEK · 2002 to 2026
$29.9M
Reovirus Attachment MechanismsR01AI118887 · NIAID · VANDERBILT UNIVERSITY MEDICAL CENTER · PI DERMODY, TERENCE S. · 2015 to 2019
$2.3M
NIAID NIH HHS R01 AI118887NIDDK NIH HHS P30 DK058404
6 · The paper itself

Abstract

Reovirus attachment protein σ1 is a trimeric molecule containing tail, body, and head domains. During infection, σ1 engages sialylated glycans and junctional adhesion molecule-A (JAM-A), triggering uptake into the endocytic compartment, where virions are proteolytically converted to infectious subvirion particles (ISVPs). Further disassembly allows σ1 release and escape of transcriptionally active reovirus cores into the cytosol. Electron microscopy has revealed a distinct conformational change in σ1 from a compact form on virions to an extended form on ISVPs. To determine the importance of σ1 conformational mobility, we used reverse genetics to introduce cysteine mutations that can cross-link σ1 by establishing disulfide bonds between structurally adjacent sites in the tail, body, and head domains. We detected phenotypic differences among the engineered viruses. A mutant with a cysteine pair in the head domain replicates with enhanced kinetics, forms large plaques, and displays increased avidity for JAM-A relative to the parental virus, mimicking properties of ISVPs. However, unlike ISVPs, particles containing cysteine mutations that cross-link the head domain uncoat and transcribe viral positive-sense RNA with kinetics similar to the parental virus and are sensitive to ammonium chloride, which blocks virion-to-ISVP conversion. Together, these data suggest that σ1 conformational flexibility modulates the efficiency of reovirus host cell attachment.

Indexed as

Virus AttachmentAnimalsCapsid ProteinsCell Adhesion MoleculesCell LineL CellsMiceMutationProtein BindingProtein ConformationReceptors, Cell SurfaceReoviridaeViral ProteinsVirionVirus InternalizationCapsid ProteinsCell Adhesion MoleculesReceptors, Cell SurfaceViral Proteinscrosslinkdisulfideglycanjunctional adhesion molecule-Areceptorreovirussialic acid

Identifiers

PMID32938765
PMCPMC7654274
OpenAlexW3087288588

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.