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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
7015
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pubmed:dateCreated |
2004-11-19
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pubmed:abstractText |
Vertebrate innate immunity provides a first line of defence against pathogens such as viruses and bacteria. Viral infection activates a potent innate immune response, which can be triggered by double-stranded (ds)RNA produced during viral replication. Here, we report that mammalian cells lacking the death-domain-containing protein FADD are defective in intracellular dsRNA-activated gene expression, including production of type I (alpha/beta) interferons, and are thus very susceptible to viral infection. The signalling pathway incorporating FADD is largely independent of Toll-like receptor 3 and the dsRNA-dependent kinase PKR, but seems to require receptor interacting protein 1 as well as Tank-binding kinase 1-mediated activation of the transcription factor IRF-3. The requirement for FADD in mammalian host defence is evocative of innate immune signalling in Drosophila, in which a FADD-dependent pathway responds to bacterial infection by activating the transcription of antimicrobial genes. These data therefore suggest the existence of a conserved pathogen recognition pathway in mammalian cells that is essential for the optimal induction of type I interferons and other genes important for host defence.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/AGFG1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Signal Transducing,
http://linkedlifedata.com/resource/pubmed/chemical/FADD protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Fadd protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Fas-Associated Death Domain Protein,
http://linkedlifedata.com/resource/pubmed/chemical/Interferon Type I,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Pore Complex Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/RIPK1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Double-Stranded,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/RNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor-Interacting Protein...,
http://linkedlifedata.com/resource/pubmed/chemical/Ripk1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/TBK1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Tbk1 protein, mouse
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
1476-4687
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
18
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pubmed:volume |
432
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
401-5
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pubmed:dateRevised |
2010-9-20
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pubmed:meshHeading |
pubmed-meshheading:15549108-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:15549108-Animals,
pubmed-meshheading:15549108-Cell Line,
pubmed-meshheading:15549108-Fas-Associated Death Domain Protein,
pubmed-meshheading:15549108-Fibroblasts,
pubmed-meshheading:15549108-Gene Deletion,
pubmed-meshheading:15549108-Gene Expression Regulation,
pubmed-meshheading:15549108-HeLa Cells,
pubmed-meshheading:15549108-Humans,
pubmed-meshheading:15549108-Immunity, Innate,
pubmed-meshheading:15549108-Interferon Type I,
pubmed-meshheading:15549108-Mice,
pubmed-meshheading:15549108-Nuclear Pore Complex Proteins,
pubmed-meshheading:15549108-Oligonucleotide Array Sequence Analysis,
pubmed-meshheading:15549108-Protein-Serine-Threonine Kinases,
pubmed-meshheading:15549108-RNA, Double-Stranded,
pubmed-meshheading:15549108-RNA, Messenger,
pubmed-meshheading:15549108-RNA-Binding Proteins,
pubmed-meshheading:15549108-Receptor-Interacting Protein Serine-Threonine Kinases,
pubmed-meshheading:15549108-Rhabdoviridae Infections,
pubmed-meshheading:15549108-Signal Transduction,
pubmed-meshheading:15549108-Vesicular stomatitis Indiana virus,
pubmed-meshheading:15549108-Virus Replication
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pubmed:year |
2004
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pubmed:articleTitle |
A FADD-dependent innate immune mechanism in mammalian cells.
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pubmed:affiliation |
Department of Microbiology and Immunology and Sylvester Comprehensive Cancer Center, University of Miami School of Medicine, Miami, Florida 33136, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.
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