| First Author | Pichlmair A | Year | 2011 |
| Journal | Nat Immunol | Volume | 12 |
| Issue | 7 | Pages | 624-30 |
| PubMed ID | 21642987 | Mgi Jnum | J:187549 |
| Mgi Id | MGI:5437411 | Doi | 10.1038/ni.2048 |
| Citation | Pichlmair A, et al. (2011) IFIT1 is an antiviral protein that recognizes 5'-triphosphate RNA. Nat Immunol 12(7):624-30 |
| abstractText | 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. |
