Titre
The antiviral adaptor proteins Cardif and Trif are processed and inactivated by caspases.
Type
article
Institution
UNIL/CHUV/Unisanté + institutions partenaires
Périodique
Auteur(s)
Rebsamen, M.
Co-première auteure/Co-premier auteur
Meylan, E.
Co-première auteure/Co-premier auteur
Curran, J.
Auteure/Auteur
Tschopp, J.
Auteure/Auteur
Liens vers les personnes
Liens vers les unités
ISSN
1350-9047
Statut éditorial
Publié
Date de publication
2008-11
Volume
15
Numéro
11
Première page
1804
Dernière page/numéro d’article
1811
Peer-reviewed
Oui
Langue
anglais
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't
Publication Status: ppublish
Publication Status: ppublish
Résumé
The outcome of a viral infection depends on the interplay between the host's capacity to trigger potent antiviral responses and viral mechanisms that counteract them. Although Toll-like receptor (TLR)-3, which recognizes virally derived double-stranded (ds) RNA, transmits downstream antiviral signaling through the TIR adaptor Trif (TICAM-1), viral RNA-sensing RIG-like helicases (RLHs) use the mitochondrial-bound CARD protein Cardif (IPS-1/MAVS/VISA). The importance of these two antiviral signaling pathways is reflected by the fact that both adaptors are inhibited through specific cleavage triggered by the hepatitis C virus serine protease NS3-4A. Here, we show that inactivation can also occur through cellular caspases activated by various pro-apoptotic signals. Upon caspase-dependent cleavage both adaptors loose their capacity to activate the transcription factors interferon regulatory factors (IRF) and NF-kappaB. Importantly, poliovirus infection triggers a caspase-dependent cleavage of Cardif, suggesting that some viruses may activate caspases not only as a mean to facilitate shedding and replication, but also to impair antiviral responses.
PID Serval
serval:BIB_65E4DCA6F4DB
PMID
Open Access
Oui
Date de création
2020-08-11T15:45:11.494Z
Date de création dans IRIS
2025-05-21T01:58:09Z