The antiviral adaptor proteins Cardif and Trif are processed and inactivated by caspases
Details
Serval ID
serval:BIB_9BA99B070A93
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
The antiviral adaptor proteins Cardif and Trif are processed and inactivated by caspases
Journal
Cell Death and Differentiation
ISSN
1350-9047
Publication state
Published
Issued date
2008
Peer-reviewed
Oui
Volume
15
Number
11
Pages
1804-1811
Language
english
Abstract
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
Keywords
Adaptor Proteins,Signal Transducing , Adaptor Proteins,Vesicular Transport , Antiviral Agents , Caspases , Hela Cells , Humans , Interferon Regulatory Factors , metabolism , Models,Biological , physiology , Poliovirus , Protein Processing,Post-Translational , Switzerland
Pubmed
Web of science
Open Access
Yes
Create date
29/01/2009 23:13
Last modification date
20/08/2019 16:02