Infection-specific phosphorylation of glutamyl-prolyl tRNA synthetase induces antiviral immunity
- Infection-specific phosphorylation of glutamyl-prolyl tRNA synthetase induces antiviral immunity
- 이철주; 이은영; 이현철; 김현권; 장송이; 박성준; 김용훈; 김정환; 황정원; 김재훈; 김태환; Abul Arif; 김선영; 최영기; 이철호; 정재유; Paul L Fox; 김성훈; 이정수; 김명희
- Issue Date
- Nature immunology
- VOL 17, NO 11-1262
- The mammalian cytoplasmic multi-tRNA synthetase complex (MSC) is a depot system that regulates non-translational cellular functions. Here we found that the MSC component glutamyl-prolyl-tRNA synthetase (EPRS) switched its function following viral infection and exhibited potent antiviral activity. Infection-specific phosphorylation of EPRS at Ser990 induced its dissociation from the MSC, after which it was guided to the antiviral signaling pathway, where it interacted with PCBP2, a negative regulator of mitochondrial antiviral signaling protein (MAVS) that is critical for antiviral immunity. This interaction blocked PCBP2-mediated ubiquitination of MAVS and ultimately suppressed viral replication. EPRS-haploid (Eprs(+/-)) mice showed enhanced viremia and inflammation and delayed viral clearance. This stimulus-inducible activation of MAVS by EPRS suggests an unexpected role for the MSC as a regulator of immune responses to viral infection
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