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About:
Ribose 2′-O-methylation provides a molecular signature for the distinction of self and non-self mRNA dependent on the RNA sensor Mda5
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schema:ScholarlyArticle
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wasabi.inria.fr
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Type:
Academic Article
research paper
schema:ScholarlyArticle
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type
Academic Article
research paper
schema:ScholarlyArticle
isDefinedBy
Covid-on-the-Web dataset
title
Ribose 2′-O-methylation provides a molecular signature for the distinction of self and non-self mRNA dependent on the RNA sensor Mda5
Creator
Thiel, Volker
Ziebuhr, John
Ludewig, Burkhard
Maier, Reinhard
Cervantes-Barragan, Luisa
Züst, Roland
Habjan, Matthias
Barchet, Winfried
Siddell, Stuart
Diamond, Michael
Neuman, Benjamin
Baker, Susan
Szretter, Kristy
source
Medline; PMC
abstract
The 5′ cap structures of higher eukaryote mRNAs have ribose 2′-O-methylation. Likewise, many viruses that replicate in the cytoplasm of eukaryotes have evolved 2′-O-methyltransferases to autonomously modify their mRNAs. However, a defined biological role for 2′-O-methylation of mRNA remains elusive. Here we show that 2′-O-methylation of viral mRNA was critically involved in subverting the induction of type I interferon. We demonstrate that human and mouse coronavirus mutants lacking 2′-O-methyltransferase activity induced higher expression of type I interferon and were highly sensitive to type I interferon. Notably, the induction of type I interferon by viruses deficient in 2′-O-methyltransferase was dependent on the cytoplasmic RNA sensor Mda5. This link between Mda5-mediated sensing of viral RNA and 2′-O-methylation of mRNA suggests that RNA modifications such as 2′-O-methylation provide a molecular signature for the discrimination of self and non-self mRNA.
has issue date
2011-01-09
(
xsd:dateTime
)
bibo:doi
10.1038/ni.1979
bibo:pmid
21217758
has license
green-oa
sha1sum (hex)
d5856d08e6923ed5366f12e5684243cf1ff98b9f
schema:url
https://doi.org/10.1038/ni.1979
resource representing a document's title
Ribose 2′-O-methylation provides a molecular signature for the distinction of self and non-self mRNA dependent on the RNA sensor Mda5
has PubMed Central identifier
PMC3182538
has PubMed identifier
21217758
schema:publication
Nature Immunology
resource representing a document's body
covid:d5856d08e6923ed5366f12e5684243cf1ff98b9f#body_text
is
schema:about
of
named entity 'SUPPLEMENTARY INFORMATION'
named entity '2'-O-methylation'
named entity 'MDA5'
named entity 'O-METHYLATION'
named entity 'RIBOSE'
named entity 'DEPENDENT'
named entity 'MOLECULAR SIGNATURE'
named entity 'SELF'
named entity 'MRNA'
named entity 'NON-SELF'
named entity 'PROVIDES'
named entity 'Ribose'
named entity 'Statistical analysis'
named entity '0.01'
named entity 'Student's t-test'
named entity 'MDA5'
named entity 'mRNA'
named entity '2'-O-methylation'
named entity 'non-self'
named entity 'non-self'
named entity 'dependent'
named entity 'mRNA'
named entity 'Ribose'
named entity 'molecular'
named entity 'MDA5'
is
part of
of
Ribose 2′-O-methylation provides a molecular signature for the distinction of self and non-self mRNA dependent on the RNA sensor Mda5
covid:d5856d08e6923ed5366f12e5684243cf1ff98b9f#body_text
The 5′ cap structures of higher eukaryote mRNAs have ribose 2′-O-methylation. Likewise, many viruses that replicate in the cytoplasm of eukaryotes have evolved 2′-O-methyltransferases to autonomously modify their mRNAs. However, a defined biological role for 2′-O-methylation of mRNA remains elusive. Here we show that 2′-O-methylation of viral mRNA was critically involved in subverting the induction of type I interferon. We demonstrate that human and mouse coronavirus mutants lacking 2′-O-methyltransferase activity induced higher expression of type I interferon and were highly sensitive to type I interferon. Notably, the induction of type I interferon by viruses deficient in 2′-O-methyltransferase was dependent on the cytoplasmic RNA sensor Mda5. This link between Mda5-mediated sensing of viral RNA and 2′-O-methylation of mRNA suggests that RNA modifications such as 2′-O-methylation provide a molecular signature for the discrimination of self and non-self mRNA.
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