Journalartikel

Autorenliste: Pichlmair, A; Lassnig, C; Eberle, CA; Górna, MW; Baumann, CL; Burkard, TR; Bürckstümmer, T; Stefanovic, A; Krieger, S; Bennett, KL; Rülicke, T; Weber, F; Colinge, J; Müller, M; Superti-Furga, G

Jahr der Veröffentlichung: 2011

Seiten: 624-630

Zeitschrift: Nature Immunology

Bandnummer: 12

Heftnummer: 7

ISSN: 1529-2908

DOI Link: https://doi.org/10.1038/ni.2048

Verlag: Nature Research

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.

Harvard-Zitierstil: Pichlmair, A., Lassnig, C., Eberle, C., Górna, M., Baumann, C., Burkard, T., et al. (2011) IFIT1 is an antiviral protein that recognizes 5′-triphosphate RNA, Nature Immunology, 12(7), pp. 624-630. https://doi.org/10.1038/ni.2048

APA-Zitierstil: Pichlmair, A., Lassnig, C., Eberle, C., Górna, M., Baumann, C., Burkard, T., Bürckstümmer, T., Stefanovic, A., Krieger, S., Bennett, K., Rülicke, T., Weber, F., Colinge, J., Müller, M., & Superti-Furga, G. (2011). IFIT1 is an antiviral protein that recognizes 5′-triphosphate RNA. Nature Immunology. 12(7), 624-630. https://doi.org/10.1038/ni.2048