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  4. Cardif is an adaptor protein in the RIG-I antiviral pathway and is targeted by hepatitis C virus
 
research article

Cardif is an adaptor protein in the RIG-I antiviral pathway and is targeted by hepatitis C virus

Meylan, Etienne  
•
Curran, Joseph
•
Hofmann, Kay
Show more
2005
Nature

Antiviral immunity against a pathogen is mounted upon recognition by the host of virally associated structures. One of these viral 'signatures', double-stranded (ds) RNA, is a replication product of most viruses within infected cells and is sensed by Toll-like receptor 3 (TLR3) and the recently identified cytosolic RNA helicases RIG-I (retinoic acid inducible gene I, also known as Ddx58) and Mda5 (melanoma differentiation-associated gene 5, also known as Ifih1 or Helicard). Both helicases detect dsRNA, and through their protein-interacting CARD domains, relay an undefined signal resulting in the activation of the transcription factors interferon regulatory factor 3 (IRF3) and NF-kappaB. Here we describe Cardif, a new CARD-containing adaptor protein that interacts with RIG-I and recruits IKKalpha, IKKbeta and IKKvarepsilon kinases by means of its C-terminal region, leading to the activation of NF-kappaB and IRF3. Overexpression of Cardif results in interferon-beta and NF-kappaB promoter activation, and knockdown of Cardif by short interfering RNA inhibits RIG-I-dependent antiviral responses. Cardif is targeted and inactivated by NS3-4A, a serine protease from hepatitis C virus known to block interferon-beta production. Cardif thus functions as an adaptor, linking the cytoplasmic dsRNA receptor RIG-I to the initiation of antiviral programmes.

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Type
research article
DOI
10.1038/nature04193
Author(s)
Meylan, Etienne  
•
Curran, Joseph
•
Hofmann, Kay
•
Moradpour, Darius
•
Binder, Marco
•
Bartenschlager, Ralf
•
Tschopp, Jürg
Date Issued

2005

Published in
Nature
Volume

437

Issue

7062

Start page

1167

End page

72

Note

Letter

Peer reviewed

NON-REVIEWED

Written at

OTHER

EPFL units
UPMEYLAN  
Available on Infoscience
April 26, 2012
Use this identifier to reference this record
https://infoscience.epfl.ch/handle/20.500.14299/79680
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