Infection-specific phosphorylation of glutamyl-prolyl tRNA synthetase induces antiviral immunity

Cited 41 time in scopus
Metadata Downloads
Title
Infection-specific phosphorylation of glutamyl-prolyl tRNA synthetase induces antiviral immunity
Author(s)
Eun Young Lee; H C Lee; Hyun-Kwan Kim; Song Yee Jang; S J Park; Yong-Hoon KimJong Hwan KimJungwon Hwang; J H Kim; T H Kim; A Arif; Seon-Young Kim; Y K Choi; C Lee; Chul Ho Lee; J U Jung; P L Fox; S Kim; J S Lee; Myung Hee Kim
Bibliographic Citation
Nature Immunology, vol. 17, no. 11, pp. 1252-1262
Publication Year
2016
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.
ISSN
1529-2908
Publisher
Springer-Nature Pub Group
DOI
http://dx.doi.org/10.1038/ni.3542
Type
Article
Appears in Collections:
Division of Biomedical Research > Microbiome Convergence Research Center > 1. Journal Articles
Division of Bio Technology Innovation > Core Research Facility & Analysis Center > 1. Journal Articles
Ochang Branch Institute > Division of National Bio-Infrastructure > Laboratory Animal Resource & Research Center > 1. Journal Articles
Files in This Item:
  • There are no files associated with this item.


Items in OpenAccess@KRIBB are protected by copyright, with all rights reserved, unless otherwise indicated.