Evidence map›Paper›PMID 26743679›Full record

ArticleVeterinary research2016

The non-structural protein μNS of piscine orthoreovirus (PRV) forms viral factory-like structures.

Hanne Merethe Haatveit, Ingvild B Nyman, Turhan Markussen, Øystein Wessel, Maria Krudtaa Dahle, Espen Rimstad

Open access · goldAbstract read
In one paragraph

Article in Veterinary research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
3.3field-weighted citation impact, top 8% 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

14 citing papers in PubMed, 28 citations in OpenAlex.

  1. Review
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  6. Evolution of theViruses · 2019
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  7. Detection of Salmonid IgM Specific to theFrontiers in immunology · 2019
    Article
  8. Article
  9. Review
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  11. Article
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  13. Article
  14. Article
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

6 authors at 2 institutions in 1 country.

Hanne Merethe HaatveitDepartment of Food Safety and Infectious Biology, Faculty of Veterinary Medicine and Biosciences, Norwegian University of Life Sciences, Postboks 8146 Dep, 0033, Oslo, Norway. hanne.merethe.haatveit@nmbu.no.
Ingvild B NymanDepartment of Food Safety and Infectious Biology, Faculty of Veterinary Medicine and Biosciences, Norwegian University of Life Sciences, Postboks 8146 Dep, 0033, Oslo, Norway. ingvild.nyman@nmbu.no.
Turhan MarkussenDepartment of Food Safety and Infectious Biology, Faculty of Veterinary Medicine and Biosciences, Norwegian University of Life Sciences, Postboks 8146 Dep, 0033, Oslo, Norway. turhan.markussen@nmbu.no.
Øystein WesselDepartment of Food Safety and Infectious Biology, Faculty of Veterinary Medicine and Biosciences, Norwegian University of Life Sciences, Postboks 8146 Dep, 0033, Oslo, Norway. oystein.wessel@nmbu.no.
Maria Krudtaa DahleDepartment of Immunology, Norwegian Veterinary Institute, Postboks 750 Sentrum, 0106, Oslo, Norway. maria.dahle@vetinst.no.
Espen RimstadDepartment of Food Safety and Infectious Biology, Faculty of Veterinary Medicine and Biosciences, Norwegian University of Life Sciences, Postboks 8146 Dep, 0033, Oslo, Norway. espen.rimstad@nmbu.no.
Norwegian University of Life Sciences · NONorwegian Veterinary Institute · NO

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Piscine orthoreovirus (PRV) is associated with heart- and skeletal muscle inflammation in farmed Atlantic salmon. The virus is ubiquitous and found in both farmed and wild salmonid fish. It belongs to the family Reoviridae, closely related to the genus Orthoreovirus. The PRV genome comprises ten double-stranded RNA segments encoding at least eight structural and two non-structural proteins. Erythrocytes are the major target cells for PRV. Infected erythrocytes contain globular inclusions resembling viral factories; the putative site of viral replication. For the mammalian reovirus (MRV), the non-structural protein μNS is the primary organizer in factory formation. The analogous PRV protein was the focus of the present study. The subcellular location of PRV μNS and its co-localization with the PRV σNS, µ2 and λ1 proteins was investigated. We demonstrated that PRV μNS forms dense globular cytoplasmic inclusions in transfected fish cells, resembling the viral factories of MRV. In co-transfection experiments with μNS, the σNS, μ2 and λ1 proteins were recruited to the globular structures. The ability of μNS to recruit other PRV proteins into globular inclusions indicates that it is the main viral protein involved in viral factory formation and pivotal in early steps of viral assembly.

Indexed as

Amino Acid SequenceAnimalsCell LineFishesGene Expression Regulation, ViralMolecular Sequence DataOrthoreovirusViral Nonstructural ProteinsVirus ReplicationViral Nonstructural Proteins

Identifiers

PMID26743679
PMCPMC4705589
OpenAlexW2225589459

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.