Lysine methylation is a post-translational modification of histone and non-histone proteins and affects numerous cellular processes. The actin histidine methyltransferase SET domain containing 3 (SETD3) is a member of the protein lysine methyltransferase (PKMT) family which catalyse the addition of methyl groups to lysine residues. However, the role of SETD3 in virus-mediated innate immune responses has rarely been investigated. In this study, zebrafish SETD3 was shown to be induced by poly(I:C) and spring viremia of carp virus (SVCV) and inhibited virus infection. Further, it was found that SETD3 directly interacted with SVCV phosphoprotein (SVCV P) in the cytoplasm of EPC cells, initiating ubiquitination to degrade the SVCV P protein via the proteasomal pathway. Interestingly, mutants lacking the SET and RSB domains were able to promote degradation of SVCV P, indicating that they are not required for SETD3 mediated degradation of SVCV P. Taken together, our study demonstrates that SETD3 is an antiviral factor which limits virus replication by promoting ubiquitination of viral phosphoprotein and subsequent protein degradation.
Zebrafish SETD3 mediated ubiquitination of phosphoprotein limits spring viremia of carp virus infection.
Xin Zhao,N. Ji,Jiahong Guo,Wenji Huang,Jianhua Feng,Yanjie Shi,Kangyong Chen,Junya Wang,Jun Zou
Published 2023 in Fish and Shellfish Immunology
ABSTRACT
PUBLICATION RECORD
- Publication year
2023
- Venue
Fish and Shellfish Immunology
- Publication date
2023-06-01
- Fields of study
Biology, Medicine, Environmental Science
- Identifiers
- External record
- Source metadata
Semantic Scholar, PubMed
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