File Download
  Links for fulltext
     (May Require Subscription)
Supplementary

Article: RAIDD Mediates TLR3 and IRF7 Driven Type i Interferon Production

TitleRAIDD Mediates TLR3 and IRF7 Driven Type i Interferon Production
Authors
KeywordsInnate immunity
RAIDD
TLR
IRF7
Issue Date2016
Citation
Cellular Physiology and Biochemistry, 2016, v. 39, n. 4, p. 1271-1280 How to Cite?
AbstractBackground/Aims: Viral infections represent a global health problem with the need for new viral therapies and better understanding of the immune response during infection. The most immediate and potent anti-viral defense mechanism is the production of type I interferon (IFN-I) which are activated rapidly following recognition of viral infection by host pathogen recognition receptors (PRR). The mechanisms of innate cellular signaling downstream of PRR activation remain to be fully understood. In the present study, we demonstrate that CASP2 and RIPK1 domain-containing adaptor with death domain (CRADD/RAIDD) is a critical component in type I IFN production. Methods: The role of RAIDD during IFN-I production was investigated using western blot, shRNA mediated lentiviral knockdown, immunoprecipitation and IFN-I driven dual luciferase assay. Results: Immunoprecipitation analysis revealed the molecular interaction of RAIDD with interferon regulatory factor 7 (IRF7) and its phosphorylating kinase IKKϵ. Using an IFN-4α driven dual luciferase analysis in RAIDD deficient cells, type I IFN activation by IKKϵ and IRF7 was dramatically reduced. Furthermore, deletion of either the caspase recruitment domain (CARD) or death domain (DD) of RAIDD inhibited IKKϵ and IRF7 mediated interferon-4α activation. Conclusion: We have identified that the adaptor molecule RAIDD coordinates IKKϵ and IRF7 interaction to ensure efficient expression of type I interferon.
Persistent Identifierhttp://hdl.handle.net/10722/292965
ISSN
2023 Impact Factor: 2.5
2023 SCImago Journal Rankings: 0.733
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorManey, Sathish Kumar-
dc.contributor.authorXu, Haifeng C.-
dc.contributor.authorHuang, Jun-
dc.contributor.authorPandyra, Aleksandra A.-
dc.contributor.authorEhlting, Christian-
dc.contributor.authorAguilar-Valenzuela, Renan-
dc.contributor.authorPozdeev, Vitaly I.-
dc.contributor.authorMcIlwain, David R.-
dc.contributor.authorZimmermann, Albert-
dc.contributor.authorBode, Johannes G.-
dc.contributor.authorHengel, Hartmut-
dc.contributor.authorKirschning, Carsten J.-
dc.contributor.authorKim, Ira R.-
dc.contributor.authorHiscott, John-
dc.contributor.authorBrenner, Dirk-
dc.contributor.authorHäussinger, Dieter-
dc.contributor.authorOhashi, Pamela S.-
dc.contributor.authorMak, Tak W.-
dc.contributor.authorLang, Karl S.-
dc.contributor.authorLang, Philipp A.-
dc.date.accessioned2020-11-17T14:57:35Z-
dc.date.available2020-11-17T14:57:35Z-
dc.date.issued2016-
dc.identifier.citationCellular Physiology and Biochemistry, 2016, v. 39, n. 4, p. 1271-1280-
dc.identifier.issn1015-8987-
dc.identifier.urihttp://hdl.handle.net/10722/292965-
dc.description.abstractBackground/Aims: Viral infections represent a global health problem with the need for new viral therapies and better understanding of the immune response during infection. The most immediate and potent anti-viral defense mechanism is the production of type I interferon (IFN-I) which are activated rapidly following recognition of viral infection by host pathogen recognition receptors (PRR). The mechanisms of innate cellular signaling downstream of PRR activation remain to be fully understood. In the present study, we demonstrate that CASP2 and RIPK1 domain-containing adaptor with death domain (CRADD/RAIDD) is a critical component in type I IFN production. Methods: The role of RAIDD during IFN-I production was investigated using western blot, shRNA mediated lentiviral knockdown, immunoprecipitation and IFN-I driven dual luciferase assay. Results: Immunoprecipitation analysis revealed the molecular interaction of RAIDD with interferon regulatory factor 7 (IRF7) and its phosphorylating kinase IKKϵ. Using an IFN-4α driven dual luciferase analysis in RAIDD deficient cells, type I IFN activation by IKKϵ and IRF7 was dramatically reduced. Furthermore, deletion of either the caspase recruitment domain (CARD) or death domain (DD) of RAIDD inhibited IKKϵ and IRF7 mediated interferon-4α activation. Conclusion: We have identified that the adaptor molecule RAIDD coordinates IKKϵ and IRF7 interaction to ensure efficient expression of type I interferon.-
dc.languageeng-
dc.relation.ispartofCellular Physiology and Biochemistry-
dc.rightsThis work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.-
dc.subjectInnate immunity-
dc.subjectRAIDD-
dc.subjectTLR-
dc.subjectIRF7-
dc.titleRAIDD Mediates TLR3 and IRF7 Driven Type i Interferon Production-
dc.typeArticle-
dc.description.naturepublished_or_final_version-
dc.identifier.doi10.1159/000447832-
dc.identifier.pmid27606466-
dc.identifier.scopuseid_2-s2.0-84986563750-
dc.identifier.volume39-
dc.identifier.issue4-
dc.identifier.spage1271-
dc.identifier.epage1280-
dc.identifier.eissn1421-9778-
dc.identifier.isiWOS:000384415000003-
dc.identifier.issnl1015-8987-

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats