Evidence map›Paper›PMID 41654495›Full record

ArticleNature communications2026

Myoferlin is a component of late-stage vRNP trafficking vesicles for enveloped RNA viruses.

Stefano Bonazza, Hannah L Turkington, Swathi Sukumar, Emily Peate, Hannah L Coutts, Joshua J Montgomery, Courtney Hawthorn, Erin M P E Getty, Olivier Touzelet, Judit Barabas and 2 more

Abstract read
In one paragraph

Article in Nature communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–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

2 citing papers in PubMed.

  1. Article
  2. Review
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

12 authors.

Stefano BonazzaWellcome-Wolfson Institute for Experimental Medicine, Queen's University Belfast, Belfast, UK.ORCID 0000-0001-9395-5620
Hannah L TurkingtonWellcome-Wolfson Institute for Experimental Medicine, Queen's University Belfast, Belfast, UK.
Swathi SukumarWellcome-Wolfson Institute for Experimental Medicine, Queen's University Belfast, Belfast, UK.ORCID 0000-0001-5729-8942
Emily PeateWellcome-Wolfson Institute for Experimental Medicine, Queen's University Belfast, Belfast, UK.
Hannah L CouttsWellcome-Wolfson Institute for Experimental Medicine, Queen's University Belfast, Belfast, UK.
Joshua J MontgomeryWellcome-Wolfson Institute for Experimental Medicine, Queen's University Belfast, Belfast, UK.
Courtney HawthornWellcome-Wolfson Institute for Experimental Medicine, Queen's University Belfast, Belfast, UK.
Erin M P E GettyWellcome-Wolfson Institute for Experimental Medicine, Queen's University Belfast, Belfast, UK.
Olivier TouzeletWellcome-Wolfson Institute for Experimental Medicine, Queen's University Belfast, Belfast, UK.
Judit BarabasWellcome-Wolfson Institute for Experimental Medicine, Queen's University Belfast, Belfast, UK.
Ultan F PowerWellcome-Wolfson Institute for Experimental Medicine, Queen's University Belfast, Belfast, UK.ORCID 0000-0003-3246-3774
David G CourtneyWellcome-Wolfson Institute for Experimental Medicine, Queen's University Belfast, Belfast, UK. david.courtney@qub.ac.uk.ORCID 0000-0002-0677-1194

Funding

EC | EU Framework Programme for Research and Innovation H2020 | H2020 Priority Excellent Science | H2020 European Research Council (H2020 Excellent Science - European Research Council) PTFLU 949506
6 · The paper itself

Abstract

The Rab11 endosomal recycling pathway is exploited by important respiratory RNA viruses such as IAV and RSV, aiding viral egress from the apical surface of polarized epithelial cells. Late in infection, Rab11-containing vesicles specifically transport viral ribonucleoprotein (vRNP) complexes towards the cell surface before packaging and budding. Rather than employing traditional Rab11-positive recycling endosomes, virus-infected cells generate remodelled Rab11-containing vesicles, as observed during IAV infection. Besides Rab11, no other conserved host co-factors have been identified among these various vRNP trafficking vesicles. Here we discover and confirm myoferlin's association with IAV vRNPs in the cytoplasm and colocalisation with Rab11 during late stages of infection. We also find that this role is conserved in late-stage vRNP trafficking of other viruses, including RSV and SeV. Myoferlin likely recruits the EHD family of proteins, which are involved in endosomal biogenesis, to these unique vRNP trafficking endosomes, highlighting myoferlin's pivotal role in viral replication.

Indexed as

Calcium-Binding ProteinsMembrane ProteinsMuscle ProteinsRibonucleoproteinsRNA VirusesTransport VesiclesViral ProteinsAnimalsDogsEndosomesHumansInfluenza A virusMadin Darby Canine Kidney CellsProtein Transportrab11 GTP-Binding Proteinsrab GTP-Binding ProteinsCalcium-Binding ProteinsMembrane ProteinsMuscle Proteinsrab11 GTP-Binding Proteinsrab GTP-Binding ProteinsRibonucleoproteinsViral Proteins

Identifiers

PMID41654495
PMCPMC12996415

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.