Peer-reviewed veterinary case report
Infection-specific phosphorylation of glutamyl-prolyl tRNA synthetase induces antiviral immunity.
- Journal:
- Nature immunology
- Year:
- 2016
- Authors:
- Lee, Eun-Young et al.
- Affiliation:
- Korea Research Institute of Bioscience and Biotechnology (KRIBB) · South Korea
- Species:
- rodent
Abstract
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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Search related cases →Original publication: https://pubmed.ncbi.nlm.nih.gov/27595231/