Evidence map›Paper›PMID 24667214›Full record

ArticlePloS one2014

Proteomics analysis of the DF-1 chicken fibroblasts infected with avian reovirus strain S1133.

Wen-Ting Chen, Yi-Le Wu, Ting Chen, Chao-Sheng Cheng, Hong-Lin Chan, Hsiu-Chuan Chou, Yi-Wen Chen, Hsien-Sheng Yin

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

6 citing papers in PubMed, 13 citations in OpenAlex.

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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 2 institutions in 2 countries.

Wen-Ting ChenInstitute of Bioinformatics and Structural Biology and College of Life Sciences, National Tsing Hua University, Hsinchu, Taiwan.
Yi-Le WuInstitute of Bioinformatics and Structural Biology and College of Life Sciences, National Tsing Hua University, Hsinchu, Taiwan.
Ting ChenInstitute of Bioinformatics and Structural Biology and College of Life Sciences, National Tsing Hua University, Hsinchu, Taiwan.
Chao-Sheng ChengInstitute of Bioinformatics and Structural Biology and College of Life Sciences, National Tsing Hua University, Hsinchu, Taiwan.
Hong-Lin ChanInstitute of Bioinformatics and Structural Biology and College of Life Sciences, National Tsing Hua University, Hsinchu, Taiwan.
Hsiu-Chuan ChouDepartment of Applied Science, National Hsinchu University of Education, Hsinchu, Taiwan.
Yi-Wen ChenInstitute of Bioinformatics and Structural Biology and College of Life Sciences, National Tsing Hua University, Hsinchu, Taiwan.
Hsien-Sheng YinInstitute of Bioinformatics and Structural Biology and College of Life Sciences, National Tsing Hua University, Hsinchu, Taiwan.
National Tsing Hua University · TWUniversity of Education, Winneba · GH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundAvian reovirus (ARV) is a member of the Orthoreovirus genus in the Reoviridae family. It is the etiological agent of several diseases, among which viral arthritis and malabsorption syndrome are the most commercially important, causing considerable economic losses in the poultry industry. Although a small but increasing number of reports have characterized some aspects of ARV infection, global changes in protein expression in ARV-infected host cells have not been examined. The current study used a proteomics approach to obtain a comprehensive view of changes in protein levels in host cells upon infection by ARV. METHODOLOGY AND PRINCIPAL

findingsThe proteomics profiles of DF-1 chicken fibroblast cells infected with ARV strain S1133 were analyzed by two-dimensional differential-image gel electrophoresis. The majority of protein expression changes (≥ 1.5 fold, p<0.05) occurred at 72 h post-infection. Matrix-assisted laser desorption ionization time-of-flight mass spectrometry identified 51 proteins with differential expression levels, including 25 that were upregulated during ARV infection and 26 that were downregulated. These proteins were divided into eight groups according to biological function: signal transduction, stress response, RNA processing, the ubiquitin-proteasome pathway, lipid metabolism, carbohydrate metabolism, energy metabolism, and cytoskeleton organization. They were further examined by immunoblotting to validate the observed alterations in protein expression. CONCLUSION/SIGNIFICANCE: This is the first report of a time-course proteomic analysis of ARV-infected host cells. Notably, all identified proteins involved in signal transduction, RNA processing, and the ubiquitin-proteasome pathway were downregulated in infected cells, whereas proteins involved in DNA synthesis, apoptosis, and energy production pathways were upregulated. In addition, other differentially expressed proteins were linked with the cytoskeleton, metabolism, redox regulation, and stress response. These proteomics data provide valuable information about host cell responses to ARV infection and will facilitate further studies of the molecular mechanisms underlying ARV pathogenesis.

Indexed as

AnimalsBiomarkersCells, CulturedChickensElectrophoresis, Gel, Two-DimensionalFibroblastsFluorescent Antibody TechniqueImmunoblottingOrthoreovirus, AvianProteomeProteomicsReoviridae InfectionsSignal TransductionSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationBiomarkersProteome

Identifiers

PMID24667214
PMCPMC3965424
OpenAlexW2067239973

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LicenceCC BY
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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.