Dataset Information

Tandem mass tag-based quantitative proteomics analysis of chicken bursa of Fabricius infected with reticuloendotheliosis virus

ABSTRACT: Reticuloendotheliosis virus (REV) is a type C avian retrovirus; which causes immunosuppression, dwarf syndrome, and lymphoma in infected hosts. In this study, we used tandem mass tag (TMT) labeling and liquid chromatography-mass spectrometry/mass spectrometry (LC-MS/MS) to characterize protein alterations in chicken bursa of Fabricius, before and after REV infection at 7, 14, 21, and 28 days. Our data showed that 1127, 999, 910 and 1138 differentially expressed proteins were significantly altered at 7, 14, 21, 28 days after REV infection, respectively. Bioinformatics analysis indicated these proteins were mainly participate in are mainly involved with immune responses, energy metabolism, cellular processes, biological regulation, metabolic processes, response to stimuli, and multicellular organismal process. Kyoto Encyclopedia of Genes and Genomes (KEGG) pathway cluster analysis showed that post-infection, proteins were enriched in the cell cycle, Wnt signaling, antigen processing and presentation, cytokine receptor interaction, Adenosine 3',5'-cyclic monophosphate signaling pathway, and NF-κB signaling. In addition, heat shock protein (HSP) levels also changed significantly after REV infection. These findings help clarify interactions between REV and the host, and provides mechanistic insights on REV-induced host immunosuppression.

INSTRUMENT(S): Q Exactive Plus

ORGANISM(S): Gallus Gallus (chicken)

SUBMITTER: Shimin Zheng

LAB HEAD: Shimin Zheng

PROVIDER: PXD024278 | Pride | 2021-09-10

REPOSITORIES: Pride

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Publications

Tandem Mass Tag-Based Quantitative Proteomic Analysis of Chicken Bursa of Fabricius Infected With Reticuloendotheliosis Virus.

Yang Dahan D Lv Xiaoping X Zhang Shujun S Zheng Shimin S

Frontiers in veterinary science 20210525

Reticuloendotheliosis virus (REV) is a type C avian retrovirus that causes immunosuppression, dwarf syndrome, and lymphoma in infected hosts. In this study, we used tandem mass tag (TMT) labeling and liquid chromatography-tandem mass spectrometry (LC-MS/MS) to characterize protein alterations in chicken bursa of Fabricius, before and after REV infection at 7, 14, 21, and 28 days. Our data showed that 1,127, 999, 910, and 1,138 differentially expressed proteins were significantly altered at 7, 14 ...[more]

PMID: 34113672

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Project description:Cystic echinococcosis (CE) is a chronic zoonosis caused by infection with the larval stage(protoscoleces, PSCs) of the cestode Echinococcus granulosus. A unique characteristic of the PSC is an ability to develop bidirectionally into an adult worm in the definitive host or into a secondary hydatid cyst in the intermediate host. Furmore, the cestode has a complex life-cycle involving different development stages but the mechanisms underpinning this development. Many studies have demonstrated that some matrix proteins undergo posttranslational modifications, including phosphorylation and glycosylation, which have important regulatory effects on the functional properties of the proteins. Systematic analysis of the proteome, the phosphorylated modified proteome and the glycosylated modified proteome of the PSCs and adult worms was performed using a proteomics strategy. A total of 6407 phosphorylation sites and 1757 proteins were quantifiable. Of those, 2032 phosphorylation sites and 770 proteins were up-regulated, and 2993 phosphorylation sites and 1217 proteins were down-regulated in the PSCs compared with the adult worms. A total of 612 N-glycosylation sites within 392 N-glycoproteins were identified. Of which, 355 N-glycosylation sites and 212 N-glycoproteins were quantifiable. Of those, 90 N-glycosylation sites and 64 N-glycoproteins were up-regulated, and 171 N-glycosylation sites and 126 N-glycoproteins were down-regulated 6407 in the PSCs compared with the adult worms. GO enrichment analysis indicated that the differently expressed phosphoproteins were mainly enriched in regulation of oxidoreduction coenzyme metabolic process, myelin sheath and RNA helicase activity, while the differently expressed N-glycoproteins were enriched in the cellular response to unfolded protein, endoplasmic reticulum lumen and nucleic acid binding. KEGG enrichment analysis indicated that the differently expressed phosphoproteins were mainly enriched in RNA transport, Hypertrophic cardiomyopathy (HCM), Glycolysis/Gluconeogenesis, HIF-1 signaling pathway and Pyruvate metabolism. while the differently expressed N-glycoproteins were enriched in PI3K-Akt signaling pathway, ECM-receptor interaction and Protein processing in endoplasmic reticulum.

Dataset Information

Tandem mass tag-based quantitative proteomics analysis of chicken bursa of Fabricius infected with reticuloendotheliosis virus

Publications

Tandem Mass Tag-Based Quantitative Proteomic Analysis of Chicken Bursa of Fabricius Infected With Reticuloendotheliosis Virus.

Similar Datasets

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