MassIVE MSV000097062

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O-GlcNAc transferase senses influenza viral RNA and restricts viral infection by integrating innate immunity and lipid metabolism

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Description

Viral infection induces robust reprogramming of metabolic pathways in host cells. However, whether host metabolic enzymes detect viral components remains unknown. Our group and others previously identified O-GlcNAc transferase (OGT), an important glucose metabolic enzyme, as a crucial mediator of the antiviral immune responses. Here, by studying a mouse model with a catalytically impaired OGT, we discover a catalytic activity-independent function of OGT in restraining influenza A virus (IAV) infection in addition to its catalytic activity-dependent effect on MAVS-mediated antiviral immunity. Biochemical studies reveal a critical antiviral effect based on OGT interacting with IAV genomic RNA that requires its N-terminal tetracopeptide repeat-4 motif. This interaction causes the translocation of nuclear OGT to cytosolic lipid droplets (LDs) to destabilize LDs-coating perilipin 2, thereby limiting LDs accumulation and in turn virus replication. In sum, our findings reveal OGT as a multifaceted metabolic sensor that integrates MAVS signaling and lipid metabolism to combat viral infection. [doi:10.25345/C51G0J66V] [dataset license: CC0 1.0 Universal (CC0 1.0)]

Keywords: Quantitative proteomics ; E3technology ; Viral infection ; Innate immunity ; DatasetType:Proteomics

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Principal Investigators:
(in alphabetical order) 		Haitao Wen, Ohio State University College of Medicine, United States
Submitting User: yayu
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