Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10971532 | Developmental & Comparative Immunology | 2015 | 7 Pages |
Abstract
The retinoic acid-inducible gene I (RIG-I) is a critical sensor for host recognition of RNA virus infection and initiation of antiviral signaling pathways in mammals. However, data on the occurrence and functions of this molecule in lower vertebrates are limited. In this study, we characterized an RIG-I homolog (DrRIG-I) from zebrafish. Structurally, this DrRIG-I shares a number of conserved functional domains/motifs with its mammalian counterparts, namely, caspase activation and recruitment domain, DExD/H box, a helicase domain, and a C-terminal domain. Functionally, stimulation with DrRIG-I CARD in zebrafish embryos significantly activated the NF-κB and IFN signaling pathways, leading to the expression of TNF-α, IL-8 and IFN-induced Mx, ISG15, and viperin. However, knockdown of TRIM25 (a pivotal activator for RIG-I receptors) significantly suppressed the induced activation of IFN signaling. Results suggested the functional conservation of RIG-I receptors in the NF-κB and IFN signaling pathways between teleosts and mammals, providing a perspective into the evolutionary history of RIG-I-mediated antiviral innate immunity.
Keywords
MDA5caspase activation and recruitment domainsAMLRepressor domainmorpholino oligonucleotidesLGP2RLRsIFN-IRIG-IORFsPRRsLMWCTDHCCTLRslaboratory of genetics and physiology 2C-terminal domainOpen reading framesacute myeloid leukemiaNF-κB signaling pathwayType I IFNretinoic acid-inducible gene ICARDHepatocellular carcinomapattern recognition receptorsToll-like receptors
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Authors
Li Nie, Ying-sheng Zhang, Wei-ren Dong, Li-xin Xiang, Jian-zhong Shao,