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  Sequestration by IFIT1 Impairs Translation of 2 ' O-unmethylated Capped RNA

Habjan, M., Hubel, P., Lacerda, L., Benda, C., Holze, C., Eberl, C. H., et al. (2013). Sequestration by IFIT1 Impairs Translation of 2 ' O-unmethylated Capped RNA. PLOS PATHOGENS, 9(10): e1003663. doi:10.1371/journal.ppat.1003663.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0015-81A0-8 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0015-81A1-6
Genre: Journal Article

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 Creators:
Habjan, Matthias1, Author              
Hubel, Philipp1, Author              
Lacerda, Livia1, Author              
Benda, Christian2, Author              
Holze, Cathleen1, Author              
Eberl, Christian H.3, Author              
Mann, Angelika1, Author              
Kindler, Eveline4, Author
Gil-Cruz, Cristina4, Author
Ziebuhr, John4, Author
Thiel, Volker4, Author
Pichlmair, Andreas1, Author              
Affiliations:
1Pichlmair, Andreas / Innate Immunity, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565166              
2Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565144              
3Mann, Matthias / Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565159              
4external, ou_persistent22              

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Free keywords: VESICULAR STOMATITIS-VIRUS; MESSENGER-RNA; RIG-I; 5'-TRIPHOSPHATE RNA; GENE-EXPRESSION; RECOGNITION; PROTEIN; IDENTIFICATION; QUANTIFICATION; METHYLATION
 Abstract: Viruses that generate capped RNA lacking 2'O methylation on the first ribose are severely affected by the antiviral activity of Type I interferons. We used proteome-wide affinity purification coupled to mass spectrometry to identify human and mouse proteins specifically binding to capped RNA with different methylation states. This analysis, complemented with functional validation experiments, revealed that IFIT1 is the sole interferon-induced protein displaying higher affinity for unmethylated than for methylated capped RNA. IFIT1 tethers a species-specific protein complex consisting of other IFITs to RNA. Pulsed stable isotope labelling with amino acids in cell culture coupled to mass spectrometry as well as in vitro competition assays indicate that IFIT1 sequesters 2'O-unmethylated capped RNA and thereby impairs binding of eukaryotic translation initiation factors to 29O-unmethylated RNA template, which results in inhibition of translation. The specificity of IFIT1 for 2'O-unmethylated RNA serves as potent antiviral mechanism against viruses lacking 2'O-methyltransferase activity and at the same time allows unperturbed progression of the antiviral program in infected cells.

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Language(s): eng - English
 Dates: 2013-10
 Publication Status: Published online
 Pages: 14
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
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Title: PLOS PATHOGENS
Source Genre: Journal
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Publ. Info: 1160 BATTERY STREET, STE 100, SAN FRANCISCO, CA 94111 USA : PUBLIC LIBRARY SCIENCE
Pages: - Volume / Issue: 9 (10) Sequence Number: e1003663 Start / End Page: - Identifier: ISSN: 1553-7374