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Article: Zebrafish TRIF, a Golgi-localized protein, participates in IFN induction and NF-κB activation

TitleZebrafish TRIF, a Golgi-localized protein, participates in IFN induction and NF-κB activation
Authors
KeywordsMolecular Sequence Numbers
Issue Date2008
PublisherAmerican Association of Immunologists. The Journal's web site is located at http://www.jimmunol.org
Citation
Journal of Immunology, 2008, v. 180 n. 8, p. 5373-5383 How to Cite?
Abstract
The antiviral immune responses were triggered by the innate immune recognition of viral infection. The type I IFNs (IFN-β and IFN-α) are the key cytokines produced upon viral infection and consequently link innate immunity with adaptive immunity. A main antiviral system in mammals is TRIF-dependent TLRs pathway, but the TRIF-independent RIG-I pathway, has also been discovered recently. In this manuscript, our study focuses on the functional characterization of zebrafish TRIF based on the comparison of its sequence and functional evolution from zebrafish to mammals. Our experimental results show that the full length cDNA of zebrafish TRIF cloned by RACE-PCR approach encodes a protein of 556 amino acids. Luciferase reporter assay confirms that zebrafish TRIF is able to induce the IFN promoter as well as activate NF-κB response promoter. The IFN induction function of zebrafish TRIF is abolished when Ala359 is mutated to Pro or His. Laser confocal microscopy shows that zebrafish TRIF is colocalized with a Golgi apparatus marker, implying its unique subcellular localization in Golgi apparatus. In zebrafish, the mRNA expression of molecules participating in RIG-I pathway are much more sensitive and specific to polyinosine-polycytidylic acid induction compared with those in TRIF-dependent antiviral pathway. The TRIF- dependent TLR4 IFN induction signaling appears not to be functional in zebrafish, since IFN expression cannot be upregulated by LPS. These two striking findings from de novo ligand induction experiments suggest a novel antiviral mechanism in zebrafish. The Journal of Immunology, 2008, 180: 5373-5383. Copyright © 2008 by The American Association of Immunologists, Inc.
Persistent Identifierhttp://hdl.handle.net/10722/90771
ISSN
2013 Impact Factor: 5.362
References

 

Author Affiliations
  1. Sun Yat-Sen University
DC FieldValueLanguage
dc.contributor.authorFan, Sen_HK
dc.contributor.authorChen, Sen_HK
dc.contributor.authorLiu, Yen_HK
dc.contributor.authorLin, Yen_HK
dc.contributor.authorLiu, Hen_HK
dc.contributor.authorGuo, Len_HK
dc.contributor.authorLin, Ben_HK
dc.contributor.authorHuang, Sen_HK
dc.contributor.authorXu, Aen_HK
dc.date.accessioned2010-09-17T10:08:08Z-
dc.date.available2010-09-17T10:08:08Z-
dc.date.issued2008en_HK
dc.identifier.citationJournal of Immunology, 2008, v. 180 n. 8, p. 5373-5383en_HK
dc.identifier.issn0022-1767en_HK
dc.identifier.urihttp://hdl.handle.net/10722/90771-
dc.description.abstractThe antiviral immune responses were triggered by the innate immune recognition of viral infection. The type I IFNs (IFN-β and IFN-α) are the key cytokines produced upon viral infection and consequently link innate immunity with adaptive immunity. A main antiviral system in mammals is TRIF-dependent TLRs pathway, but the TRIF-independent RIG-I pathway, has also been discovered recently. In this manuscript, our study focuses on the functional characterization of zebrafish TRIF based on the comparison of its sequence and functional evolution from zebrafish to mammals. Our experimental results show that the full length cDNA of zebrafish TRIF cloned by RACE-PCR approach encodes a protein of 556 amino acids. Luciferase reporter assay confirms that zebrafish TRIF is able to induce the IFN promoter as well as activate NF-κB response promoter. The IFN induction function of zebrafish TRIF is abolished when Ala359 is mutated to Pro or His. Laser confocal microscopy shows that zebrafish TRIF is colocalized with a Golgi apparatus marker, implying its unique subcellular localization in Golgi apparatus. In zebrafish, the mRNA expression of molecules participating in RIG-I pathway are much more sensitive and specific to polyinosine-polycytidylic acid induction compared with those in TRIF-dependent antiviral pathway. The TRIF- dependent TLR4 IFN induction signaling appears not to be functional in zebrafish, since IFN expression cannot be upregulated by LPS. These two striking findings from de novo ligand induction experiments suggest a novel antiviral mechanism in zebrafish. The Journal of Immunology, 2008, 180: 5373-5383. Copyright © 2008 by The American Association of Immunologists, Inc.en_HK
dc.languageengen_HK
dc.publisherAmerican Association of Immunologists. The Journal's web site is located at http://www.jimmunol.orgen_HK
dc.relation.ispartofJournal of Immunologyen_HK
dc.subjectMolecular Sequence Numbersen_HK
dc.titleZebrafish TRIF, a Golgi-localized protein, participates in IFN induction and NF-κB activationen_HK
dc.typeArticleen_HK
dc.identifier.emailLin, B:blin@hku.hken_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.scopuseid_2-s2.0-45949089813en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-45949089813&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume180en_HK
dc.identifier.issue8en_HK
dc.identifier.spage5373en_HK
dc.identifier.epage5383en_HK
dc.identifier.eissn1550-6606-

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