2. Academic Validation
  3. Zebrafish phd3 Negatively Regulates Antiviral Responses via Suppression of Irf7 Transactivity Independent of Its Prolyl Hydroxylase Activity

Zebrafish phd3 Negatively Regulates Antiviral Responses via Suppression of Irf7 Transactivity Independent of Its Prolyl Hydroxylase Activity

  • J Immunol. 2020 Aug 15;205(4):1135-1146. doi: 10.4049/jimmunol.1900902.
Guangqing Yu 1,  Xiong Li 1,  Ziwen Zhou 1,  Jinhua Tang 1,  Jing Wang 1,  Xing Liu 1,  Sijia Fan 1,  Gang Ouyang 1,  Wuhan Xiao 2
Affiliations

Affiliations

  • 1 State Key Laboratory of Freshwater Ecology and Biotechnology, Institute of Hydrobiology, Chinese Academy of Sciences, Wuhan 430072, People's Republic of China; The Key Laboratory of Aquaculture Disease Control, Ministry of Agriculture, Wuhan 430072, People's Republic of China; The Innovation Academy of Seed Design, Chinese Academy of Sciences, Wuhan 430072, People's Republic of China; and University of Chinese Academy of Sciences, Beijing 100049, People's Republic of China.
  • 2 State Key Laboratory of Freshwater Ecology and Biotechnology, Institute of Hydrobiology, Chinese Academy of Sciences, Wuhan 430072, People's Republic of China; The Key Laboratory of Aquaculture Disease Control, Ministry of Agriculture, Wuhan 430072, People's Republic of China; The Innovation Academy of Seed Design, Chinese Academy of Sciences, Wuhan 430072, People's Republic of China; and University of Chinese Academy of Sciences, Beijing 100049, People's Republic of China w-xiao@ihb.ac.cn.
PMID: 32669312 DOI: 10.4049/jimmunol.1900902
Abstract

Prolyl hydroxylase domain (PHD)-containing Enzyme 3 belongs to the Caenorhabditis elegans gene egl-9 family of prolyl hydroxylases, which has initially been revealed to hydroxylate hypoxia-inducible factor α (HIF-α) and mediate HIF-α degradation. In addition to modulating its target function by hydroxylation, PHD3 has been also shown to influence its binding partners' function independent of its prolyl hydroxylase activity. In this study, we report that overexpression of zebrafish phd3 suppresses cellular Antiviral response. Moreover, disruption of phd3 in zebrafish increases the survival rate upon spring viremia of carp virus exposure. Further assays indicate that phd3 interacts with irf7 through the C-terminal IRF association domain of irf7 and diminishes K63-linked ubiquitination of irf7. However, the enzymatic activity of phd3 is not required for phd3 to inhibit irf7 transactivity. This study provides novel insights into phd3 function and sheds new LIGHT on the regulation of irf7 in retinoic acid-inducible gene I-like receptor signaling.

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