ZFIN ID: ZDB-PUB-200710-21
Zebrafish prmt3 negatively regulates antiviral responses
Zhu, J., Liu, X., Cai, X., Ouyang, G., Zha, H., Zhou, Z., Liao, Q., Wang, J., Xiao, W.
Date: 2020
Source: FASEB journal : official publication of the Federation of American Societies for Experimental Biology   34(8): 10212-10227 (Journal)
Registered Authors: Ouyang, Gang, Xiao, Wuhan
Keywords: prmt3, GCRV, SVCV, innate immunity, zebrafish
MeSH Terms:
  • Animals
  • Antiviral Agents/immunology*
  • Cells, Cultured
  • Histones/genetics
  • Histones/immunology
  • Immunity, Innate/genetics
  • Immunity, Innate/immunology
  • Isoquinolines/immunology
  • Methylation
  • Phosphorylation/genetics
  • Phosphorylation/immunology
  • Protein Processing, Post-Translational/genetics
  • Protein Processing, Post-Translational/immunology
  • Protein-Arginine N-Methyltransferases/genetics*
  • Protein-Arginine N-Methyltransferases/immunology*
  • Rhabdoviridae/immunology
  • Rhabdoviridae Infections/genetics
  • Rhabdoviridae Infections/immunology
  • Up-Regulation/genetics
  • Up-Regulation/immunology
  • Virus Diseases/genetics
  • Virus Diseases/immunology
  • Virus Diseases/virology
  • Zebrafish/genetics*
  • Zebrafish/immunology*
  • Zebrafish/virology
  • Zinc Fingers/genetics
  • Zinc Fingers/immunology
PubMed: 32643209 Full text @ FASEB J.
Arginine methylation catalyzed by protein arginine methyltransferases (PRMT) is a common post-translational modification in histone and nonhistone proteins, which regulates many cellular functions. Protein arginine methyltransferase 3 (prmt3), a type I arginine methyltransferase, has been shown to carry out the formation of stable monomethylarginine as an intermediate before the establishment of asymmetric dimethylarginine. To date, however, the role of PRMT3 in antiviral innate immunity has not been elucidated. This study showed that zebrafish prmt3 was upregulated by virus infection and that the overexpression of prmt3 suppressed cellular antiviral response. The PRMT3 inhibitor, SGC707, enhanced antiviral capability. Consistently, prmt3-null zebrafish were more resistant to Spring Viremia of Carp Virus (SVCV) and Grass Carp Reovirus (GCRV) infection. Further assays showed that the overexpression of prmt3 diminished the phosphorylation of irf3 and prmt3 interacted with rig-i. In addition, both zinc-finger domain and catalytic domain of prmt3 were required for the suppressive function of prmt3 on IFN activation. Our findings suggested that zebrafish prmt3 negatively regulated the antiviral responses, implicating the vital role of prmt3-or even arginine methylation-in antiviral innate immunity.