Key result
Classical and novel duck reovirus infections significantly altered the phosphorylation levels of 392 sites on 288 proteins and 484 sites on 342 proteins, respectively, in duckling spleen tissues.
Why the study?
The roles of protein phosphorylation in the immune responses of ducklings to Classic/Novel duck reovirus infections are largely unknown.
Duck reovirus infection significantly alters the phosphoproteome of duck spleen tissue, particularly affecting proteins involved in blood coagulation and pattern-recognition receptor signaling pathways.
Phosphoproteomic shifts mark immune pathway activation in infected ducklings; leaves open functional validation and translation to disease models.
Duck reovirus (DRV) is a fatal member of the genus Orthoreovirus in the family Reoviridae. The disease caused by DRV leads to huge economic losses to the duck industry. Post-translational modification is an efficient strategy to enhance the immune responses to virus infection. However, the roles of protein phosphorylation in the responses of ducklings to Classic/Novel DRV (C/NDRV) infections are largely unknown. Using a high-resolution LC-MS/MS integrated to highly sensitive immune-affinity antibody method, phosphoproteomes of Cairna moschata spleen tissues under the C/NDRV infections were analyzed, producing a total of 8,504 phosphorylation sites on 2,853 proteins. After normalization with proteomic data, 392 sites on 288 proteins and 484 sites on 342 proteins were significantly changed under the C/NDRV infections, respectively. To characterize the differentially phosphorylated proteins (DPPs), a systematic bioinformatics analyses including Gene Ontology annotation, domain annotation, subcellular localization, and Kyoto Encyclopedia of Genes and Genomes pathway annotation were performed. Two important serine protease system-related proteins, coagulation factor X and fibrinogen α-chain, were identified as phosphorylated proteins, suggesting an involvement of blood coagulation under the C/NDRV infections. Furthermore, 16 proteins involving the intracellular signaling pathways of pattern-recognition receptors were identified as phosphorylated proteins. Changes in the phosphorylation levels of MyD88, NF-κB, RIP1, MDA5 and IRF7 suggested a crucial role of protein phosphorylation in host immune responses of C. moschata. Our study provides new insights into the responses of ducklings to the C/NDRV infections at PTM level.
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Yun et al. (2020) studied Duck reovirus (DRV) infection (n=27). Classical/novel duck reovirus (C/NDRV) infection vs. Sterile medium (un-infected) was evaluated on Differentially phosphorylated proteins (DPPs). Classical and novel duck reovirus infections significantly altered the phosphorylation levels of 392 sites on 288 proteins and 484 sites on 342 proteins, respectively, in duckling spleen tissues.
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