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Open AccessArticle

Comparative Proteomic Analysis of Lysine Acetylation in Fish CIK Cells Infected with Aquareovirus

1
State Key Laboratory of Virology, Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan 430071, China
2
State Key Laboratory of Freshwater Ecology and Biotechnology, Institute of Hydrobiology, Chinese Academy of Sciences, Wuhan 430072, China
3
Jingjie PTM BioLab (Hangzhou) Co., Ltd., Hangzhou 310018, China
*
Author to whom correspondence should be addressed.
Int. J. Mol. Sci. 2017, 18(11), 2419; https://doi.org/10.3390/ijms18112419
Received: 13 October 2017 / Revised: 10 November 2017 / Accepted: 12 November 2017 / Published: 14 November 2017
(This article belongs to the Section Biochemistry)
Grass carp (Ctenopharyngodon idellus) is an important worldwide commercial freshwater culture species. However, grass carp reovirus (GCRV) causes serious hemorrhagic disease in fingerlings and yearlings of fishes. To understand the molecular pathogenesis of host cells during GCRV infection, intensive proteomic quantification analysis of lysine acetylation in Ctenopharyngodon idella kidney (CIK) cells was performed. Using dimethylation labeling-based quantitative proteomics, 832 acetylated proteins with 1391 lysine acetylation sites were identified in response to GCRV infection, among which 792 proteins with 1323 sites were quantifiable. Bioinformatics analysis showed that differentially expressed lysine acetylated proteins are involved in diverse cellular processes and associated with multifarious functions, suggesting that extensive intracellular activities were changed upon viral infection. In addition, extensive alterations on host–protein interactions at the lysine acetylation level were also detected. Further biological experiments showed that the histone deacetylases (HDAC) inhibitor suberoylanilide hydroxamic acid (SAHA) could significantly suppress the GCRV replication. To our knowledge, this is the first to reveal the proteome-wide changes in host cell acetylome with aquatic virus infection. The results provided in this study laid a basis for further understanding the host response to aquareovirus infection in the post-translational modification aspect by regulating cell lysine acetylation conducive to viral replication. View Full-Text
Keywords: comparative proteomics; Ctenopharyngodon idella kidney cells; aquareovirus infection; lysine acetylation comparative proteomics; Ctenopharyngodon idella kidney cells; aquareovirus infection; lysine acetylation
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MDPI and ACS Style

Guo, H.; Zhang, J.; Wang, Y.; Bu, C.; Zhou, Y.; Fang, Q. Comparative Proteomic Analysis of Lysine Acetylation in Fish CIK Cells Infected with Aquareovirus. Int. J. Mol. Sci. 2017, 18, 2419. https://doi.org/10.3390/ijms18112419

AMA Style

Guo H, Zhang J, Wang Y, Bu C, Zhou Y, Fang Q. Comparative Proteomic Analysis of Lysine Acetylation in Fish CIK Cells Infected with Aquareovirus. International Journal of Molecular Sciences. 2017; 18(11):2419. https://doi.org/10.3390/ijms18112419

Chicago/Turabian Style

Guo, Hong; Zhang, Jie; Wang, Yaping; Bu, Chen; Zhou, Yanyan; Fang, Qin. 2017. "Comparative Proteomic Analysis of Lysine Acetylation in Fish CIK Cells Infected with Aquareovirus" Int. J. Mol. Sci. 18, no. 11: 2419. https://doi.org/10.3390/ijms18112419

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