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      IFIT1 is an antiviral protein that recognizes 5'-triphosphate RNA.

      Nature immunology

      immunology, RNA, Viral, Mice, Inbred C57BL, Mice, Male, Humans, HeLa Cells, HEK293 Cells, Female, genetics, chemistry, Carrier Proteins, Arginine, Animals, Viruses

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          Abstract

          Antiviral innate immunity relies on the recognition of microbial structures. One such structure is viral RNA that carries a triphosphate group on its 5' terminus (PPP-RNA). By an affinity proteomics approach with PPP-RNA as the 'bait', we found that the antiviral protein IFIT1 (interferon-induced protein with tetratricopeptide repeats 1) mediated binding of a larger protein complex containing other IFIT family members. IFIT1 bound PPP-RNA with nanomolar affinity and required the arginine at position 187 in a highly charged carboxy-terminal groove of the protein. In the absence of IFIT1, the growth and pathogenicity of viruses containing PPP-RNA was much greater. In contrast, IFIT proteins were dispensable for the clearance of pathogens that did not generate PPP-RNA. On the basis of this specificity and the great abundance of IFIT proteins after infection, we propose that the IFIT complex antagonizes viruses by sequestering specific viral nucleic acids.

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          Journal
          10.1038/ni.2048
          21642987

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