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Zebrafish prmt3 negatively regulates antiviral responses
Author(s) -
Zhu Junji,
Liu Xing,
Cai Xiaolian,
Ouyang Gang,
Zha Huangyuan,
Zhou Ziwen,
Liao Qian,
Wang Jing,
Xiao Wuhan
Publication year - 2020
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fj.201902569r
Subject(s) - zebrafish , biology , microbiology and biotechnology , genetics , gene
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.