Evidence map›Paper›PMID 33846319›Full record

ArticleNature communications2021

Reovirus directly engages integrin to recruit clathrin for entry into host cells.

Melanie Koehler, Simon J L Petitjean, Jinsung Yang, Pavithra Aravamudhan, Xayathed Somoulay, Cristina Lo Giudice, Mégane A Poncin, Andra C Dumitru, Terence S Dermody, David Alsteens

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
7.1field-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

28 citing papers in PubMed, 53 citations in OpenAlex.

  1. Article
  2. Article
  3. Alpha-Glucosidase ofViruses · 2026
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  13. Article
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  15. Article
  16. Review
  17. Host Subcellular Organelles: Targets of Viral Manipulation.International journal of molecular sciences · 2024
    Review
  18. Article
  19. Article
  20. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors at 3 institutions in 2 countries.

Melanie Koehler *Louvain Institute of Biomolecular Science and Technology, Université catholique de Louvain, Louvain-la-Neuve, Belgium.ORCID http://orcid.org/0000-0003-3042-1749
Simon J L Petitjean *Louvain Institute of Biomolecular Science and Technology, Université catholique de Louvain, Louvain-la-Neuve, Belgium.
Jinsung Yang *Louvain Institute of Biomolecular Science and Technology, Université catholique de Louvain, Louvain-la-Neuve, Belgium.ORCID http://orcid.org/0000-0002-9731-1002
Pavithra AravamudhanDepartment of Pediatrics, University of Pittsburgh School of Medicine, Pittsburgh, PA, USA.
Xayathed SomoulayDepartment of Pediatrics, University of Pittsburgh School of Medicine, Pittsburgh, PA, USA.
Cristina Lo GiudiceLouvain Institute of Biomolecular Science and Technology, Université catholique de Louvain, Louvain-la-Neuve, Belgium.ORCID http://orcid.org/0000-0002-5346-7638
Mégane A PoncinLouvain Institute of Biomolecular Science and Technology, Université catholique de Louvain, Louvain-la-Neuve, Belgium.
Andra C DumitruLouvain Institute of Biomolecular Science and Technology, Université catholique de Louvain, Louvain-la-Neuve, Belgium.
Terence S DermodyDepartment of Pediatrics, University of Pittsburgh School of Medicine, Pittsburgh, PA, USA. terence.dermody@chp.edu.
David AlsteensLouvain Institute of Biomolecular Science and Technology, Université catholique de Louvain, Louvain-la-Neuve, Belgium. david.alsteens@uclouvain.be.ORCID http://orcid.org/0000-0001-9229-113X
UCLouvain · BEUniversity of Pittsburgh · USWalloon Excellence in Lifesciences and Biotechnology · BE

Funding

MOLECULAR BASIS OF REOVIRUS PATHOGENESISR01AI038296 · NIAID · VANDERBILT UNIVERSITY · PI DERMODY, TERENCE S. · 1996 to 2019
$3.3M
Reovirus Attachment MechanismsR01AI118887 · NIAID · VANDERBILT UNIVERSITY MEDICAL CENTER · PI DERMODY, TERENCE S. · 2015 to 2019
$2.3M
NIAID NIH HHS R01 AI038296NIAID NIH HHS R01 AI118887
6 · The paper itself

Abstract

Reovirus infection requires the concerted action of viral and host factors to promote cell entry. After interaction of reovirus attachment protein σ1 with cell-surface carbohydrates and proteinaceous receptors, additional host factors mediate virus internalization. In particular, β1 integrin is required for endocytosis of reovirus virions following junctional adhesion molecule A (JAM-A) binding. While integrin-binding motifs in the surface-exposed region of reovirus capsid protein λ2 are thought to mediate integrin interaction, evidence for direct β1 integrin-reovirus interactions and knowledge of how integrins function to mediate reovirus entry is lacking. Here, we use single-virus force spectroscopy and confocal microscopy to discover a direct interaction between reovirus and β1 integrins. Comparison of interactions between reovirus disassembly intermediates as well as mutants and β1 integrin show that λ2 is the integrin ligand. Finally, using fluidic force microscopy, we demonstrate a functional role for β1 integrin interaction in promoting clathrin recruitment to cell-bound reovirus. Our study demonstrates a direct interaction between reovirus and β1 integrins and offers insights into the mechanism of reovirus cell entry. These results provide new perspectives for the development of efficacious antiviral therapeutics and the engineering of improved viral gene delivery and oncolytic vectors.

Indexed as

Host-Pathogen InteractionsAnimalsBinding SitesCapsidCationsCell LineCell MembraneClathrinEndocytosisIntegrin beta1KineticsMiceN-Acetylneuraminic AcidPoint MutationProtein BindingReoviridaeCationsClathrinIntegrin beta1N-Acetylneuraminic AcidViral Proteins

Identifiers

PMID33846319
PMCPMC8041799
OpenAlexW3153071425

What OpenQuestion 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 OpenQuestion graph.