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      5'-Triphosphate RNA is the ligand for RIG-I.

      Science (New York, N.Y.)

      Virus Replication, Animals, Cell Line, Cells, Cultured, Cytosol, metabolism, virology, DEAD-box RNA Helicases, DNA-Directed RNA Polymerases, Humans, Interferon-alpha, biosynthesis, Interferon-beta, Ligands, Mice, Monocytes, Oligoribonucleotides, Phosphates, Phosphorylation, RNA, chemistry, RNA Caps, RNA, Double-Stranded, RNA, Viral, Rabies virus, genetics, immunology, physiology, Transcription, Genetic, Transfection, Viral Proteins

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          Abstract

          The structural basis for the distinction of viral RNA from abundant self RNA in the cytoplasm of virally infected cells is largely unknown. We demonstrated that the 5'-triphosphate end of RNA generated by viral polymerases is responsible for retinoic acid-inducible protein I (RIG-I)-mediated detection of RNA molecules. Detection of 5'-triphosphate RNA is abrogated by capping of the 5'-triphosphate end or by nucleoside modification of RNA, both occurring during posttranscriptional RNA processing in eukaryotes. Genomic RNA prepared from a negative-strand RNA virus and RNA prepared from virus-infected cells (but not from noninfected cells) triggered a potent interferon-alpha response in a phosphatase-sensitive manner. 5'-triphosphate RNA directly binds to RIG-I. Thus, uncapped 5'-triphosphate RNA (now termed 3pRNA) present in viruses known to be recognized by RIG-I, but absent in viruses known to be detected by MDA-5 such as the picornaviruses, serves as the molecular signature for the detection of viral infection by RIG-I.

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          Journal
          10.1126/science.1132505
          17038590

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