We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
IFIT1 is an antiviral protein that recognizes 5'-triphosphate RNA.
- Authors
Pichlmair, Andreas; Lassnig, Caroline; Eberle, Carol-Ann; Górna, Maria W; Baumann, Christoph L; Burkard, Thomas R; Bürckstümmer, Tilmann; Stefanovic, Adrijana; Krieger, Sigurd; Bennett, Keiryn L; Rülicke, Thomas; Weber, Friedemann; Colinge, Jacques; Müller, Mathias; Superti-Furga, Giulio
- 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.
- Publication
Nature immunology, 2011, Vol 12, Issue 7, p624
- ISSN
1529-2916
- Publication type
Journal Article
- DOI
10.1038/ni.2048