Evidence map›Paper›PMID 25556234›Full record

ArticleMolecular & cellular proteomics : MCP2015

New host factors important for respiratory syncytial virus (RSV) replication revealed by a novel microfluidics screen for interactors of matrix (M) protein.

Sarit Kipper, Samar Hamad, Leon Caly, Dorit Avrahami, Eran Bacharach, David A Jans, Doron Gerber, Monika Bajorek

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing 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

33 citing papers in PubMed, 53 citations in OpenAlex.

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  16. Role of Mitochondria in Viral Infections.Life (Basel, Switzerland) · 2021
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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 4 institutions in 3 countries.

Sarit KipperFrom the ‡Nanotechnology Institute, Mina and Evrard Goodman Faculty of Life Sciences, Bar Ilan University, Ramat Gan, Israel;
Samar Hamad§Section of Virology, Faculty of Medicine, Imperial College London, London, UK;
Leon Caly¶Department of Biochemistry and Molecular Biology, Monash University, Melbourne, Australia;
Dorit AvrahamiFrom the ‡Nanotechnology Institute, Mina and Evrard Goodman Faculty of Life Sciences, Bar Ilan University, Ramat Gan, Israel;
Eran Bacharach‖Department of Cell Research and Immunology, Tel Aviv University, Israel.
David A Jans¶Department of Biochemistry and Molecular Biology, Monash University, Melbourne, Australia;
Doron GerberFrom the ‡Nanotechnology Institute, Mina and Evrard Goodman Faculty of Life Sciences, Bar Ilan University, Ramat Gan, Israel; Doron.Gerber@biu.ac.il m.bajorek@imperial.ac.uk.
Monika Bajorek§Section of Virology, Faculty of Medicine, Imperial College London, London, UK; Doron.Gerber@biu.ac.il m.bajorek@imperial.ac.uk.
Bar-Ilan University · ILImperial College London · GBMonash University · AUTel Aviv University · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Although human respiratory syncytial virus (RSV) is the most common cause of bronchiolitis and pneumonia in infants and elderly worldwide, there is no licensed RSV vaccine or effective drug treatment available. The RSV Matrix protein plays key roles in virus life cycle, being found in the nucleus early in infection in a transcriptional inhibitory role, and later localizing in viral inclusion bodies before coordinating viral assembly and budding at the plasma membrane. In this study, we used a novel, high throughput microfluidics platform and custom human open reading frame library to identify novel host cell binding partners of RSV matrix. Novel interactors identified included proteins involved in host transcription regulation, the innate immunity response, cytoskeletal regulation, membrane remodeling, and cellular trafficking. A number of these interactions were confirmed by immunoprecipitation and cellular colocalization approaches. Importantly, the physiological significance of matrix interaction with the actin-binding protein cofilin 1, caveolae protein Caveolin 2, and the zinc finger protein ZNF502 was confirmed. siRNA knockdown of the host protein levels resulted in reduced RSV virus production in infected cells. These results have important implications for future antiviral strategies aimed at targets of RSV matrix in the host cell.

Indexed as

AnimalsCarrier ProteinsCaveolin 2Cell LineCell NucleusChlorocebus aethiopsCofilin 1Gene LibraryHEK293 CellsHumansMicrofluidic Analytical TechniquesNuclear ProteinsOpen Reading FramesRespiratory Syncytial VirusesVero CellsViral Matrix ProteinsCarrier ProteinsCAV2 protein, humanCaveolin 2CFL1 protein, humanCofilin 1Nuclear ProteinsViral Matrix ProteinsZNF502 protein, human

Identifiers

PMID25556234
PMCPMC4349975
OpenAlexW2124107211

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.