Abstract
The innate immune system provides a rapid protective response against a wide range of cellular insults sensed by the host as danger signals, including those associated with viral infections. The NLRP3 inflammasome is a multiprotein complex that assembles in response to danger signals, including those generated by viruses, triggering self-cleavage of procaspase-1 and subsequent processing of proinflammatory cytokines. Precisely how viruses and inflammatory cells interact to control this process remains incompletely understood. The 2-prime, 5-prime oligoadenylate synthetase (OAS)/RNase L system is a component of the interferon-induced antiviral response that senses double-stranded RNA and activates endoribonuclease RNase L to cleave viral and cellular RNAs. We will report involvement of the mammalian OAS/RNase L system in viral activation of the NLRP3 inflammasome in mouse bone marrow-derived dendritic cells and in human THP-1-derived macrophages. Furthermore, RNase L deficiency reduced IL-1 β production in influenza A virus-infected mice. The signaling pathway includes RNA cleavage products with 2-prime, 3-prime-cyclic phosphorylated termini, DExD/H-box helicase, DHX33, and the mitochondrial adapter protein, MAVS. Data suggest that RNA cleavage events catalyzed by RNase L are required for optimal inflammasome activation during viral infections.
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