Litcius/Paper detail

The US3 Kinase of Herpes Simplex Virus Phosphorylates the RNA Sensor RIG-I To Suppress Innate Immunity

Michiel van Gent, Jessica J. Chiang, Santoshi Muppala, Cindy Chiang, Walid Azab, Lisa Kattenhorn, David M. Knipe, Nikolaus Osterrieder, Michaela U. Gack

2021Journal of Virology28 citationsDOIOpen Access PDF

Abstract

Herpes simplex virus 1 (HSV-1) establishes lifelong latency in the majority of the human population worldwide. HSV-1 occasionally reactivates to produce infectious virus and to facilitate dissemination. While often remaining subclinical, both primary infection and reactivation occasionally cause debilitating eye diseases, which can lead to blindness, as well as life-threatening encephalitis and newborn infections. To identify new therapeutic targets for HSV-1-induced diseases, it is important to understand the HSV-1-host interactions that may influence infection outcome and disease. Our work uncovered direct phosphorylation of the pathogen sensor RIG-I by alphaherpesvirus-encoded kinases as a novel viral immune escape strategy and also underscores the importance of RNA sensors in surveilling DNA virus infection.

Topics & Concepts

BiologyPhosphorylationSignal transductionHerpes simplex virusInnate immune systemCell biologyKinaseInterferonProtein kinase RPopulationRIG-ISmall interfering RNAVirologyIκB kinaseMAP2K7Phosphorylation cascadeProtein kinase AProinflammatory cytokineInterferon type IMeasles virusMolecular biologySignal transducing adaptor proteininterferon and immune responsesHerpesvirus Infections and TreatmentsNF-κB Signaling Pathways