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- W4380354414 endingPage "2386.e15" @default.
- W4380354414 startingPage "2367" @default.
- W4380354414 abstract "Epstein-Barr virus (EBV) causes infectious mononucleosis, triggers multiple sclerosis, and is associated with 200,000 cancers/year. EBV colonizes the human B cell compartment and periodically reactivates, inducing expression of 80 viral proteins. However, much remains unknown about how EBV remodels host cells and dismantles key antiviral responses. We therefore created a map of EBV-host and EBV-EBV interactions in B cells undergoing EBV replication, uncovering conserved herpesvirus versus EBV-specific host cell targets. The EBV-encoded G-protein-coupled receptor BILF1 associated with MAVS and the UFM1 E3 ligase UFL1. Although UFMylation of 14-3-3 proteins drives RIG-I/MAVS signaling, BILF1-directed MAVS UFMylation instead triggered MAVS packaging into mitochondrial-derived vesicles and lysosomal proteolysis. In the absence of BILF1, EBV replication activated the NLRP3 inflammasome, which impaired viral replication and triggered pyroptosis. Our results provide a viral protein interaction network resource, reveal a UFM1-dependent pathway for selective degradation of mitochondrial cargo, and highlight BILF1 as a novel therapeutic target." @default.
- W4380354414 created "2023-06-13" @default.
- W4380354414 creator A5018388583 @default.
- W4380354414 creator A5018600247 @default.
- W4380354414 creator A5057640400 @default.
- W4380354414 creator A5060656744 @default.
- W4380354414 creator A5074992735 @default.
- W4380354414 creator A5085265759 @default.
- W4380354414 date "2023-07-01" @default.
- W4380354414 modified "2023-09-25" @default.
- W4380354414 title "An Epstein-Barr virus protein interaction map reveals NLRP3 inflammasome evasion via MAVS UFMylation" @default.
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