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      RIG-I-mediated antiviral responses to single-stranded RNA bearing 5'-phosphates.

      Science (New York, N.Y.)

      Animals, Cell Line, Cells, Cultured, Cytoplasm, metabolism, virology, DEAD-box RNA Helicases, genetics, Dendritic Cells, Encephalomyocarditis virus, immunology, Genome, Viral, Humans, Immunity, Innate, Influenza A virus, physiology, Interferon-alpha, biosynthesis, Interferon-beta, Mice, Mice, Inbred C57BL, Phosphates, Phosphorylation, RNA Caps, RNA, Double-Stranded, RNA, Viral, chemistry, Recombinant Fusion Proteins, Transfection, Vesicular stomatitis Indiana virus, Viral Nonstructural Proteins, Virus Replication

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          Abstract

          Double-stranded RNA (dsRNA) produced during viral replication is believed to be the critical trigger for activation of antiviral immunity mediated by the RNA helicase enzymes retinoic acid-inducible gene I (RIG-I) and melanoma differentiation-associated gene 5 (MDA5). We showed that influenza A virus infection does not generate dsRNA and that RIG-I is activated by viral genomic single-stranded RNA (ssRNA) bearing 5'-phosphates. This is blocked by the influenza protein nonstructured protein 1 (NS1), which is found in a complex with RIG-I in infected cells. These results identify RIG-I as a ssRNA sensor and potential target of viral immune evasion and suggest that its ability to sense 5'-phosphorylated RNA evolved in the innate immune system as a means of discriminating between self and nonself.

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          Journal
          17038589
          10.1126/science.1132998

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