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  • Title: Daxx from Pacific white shrimp Litopenaeus vannamei is involved in activation of NF-κB pathway.
    Author: Yan M, Tang J, Liang Q, Zhu G, Li H, Li C, Weng S, He J, Xu X.
    Journal: Fish Shellfish Immunol; 2015 Aug; 45(2):443-53. PubMed ID: 25917972.
    Abstract:
    Death domain-associated factor 6 (Daxx) is a Fas-binding protein that mediates the activation of Jun amino-terminal kinase (JNK) pathway and Fas-induced apoptosis. In this study, a crustacean Daxx (LvDaxx) was firstly cloned and identified from Pacific white shrimp Litopenaeus vannamei. The LvDaxx cDNA was 2644 bp in length with an Open Reading Frame (ORF) of 2217 bp. Sequence analysis indicated that LvDaxx contained a single Daxx domain and two nuclear localization signals (NLSs) and shared a similarity with Drosophila melanogaster Daxx. LvDaxx was a nuclear-localized protein that was expressed highest in hemocytes and could be up-regulated in pathogen- and stimulant-challenge shrimps. LvDaxx could activate the artificial promoter containing an NF-κB binding site and the promoters of white spot syndrome virus (WSSV) ie1 gene and arthropod antimicrobial peptides (AMPs), suggesting LvDaxx could be involved in the activation of the NF-κB pathway. Knock-down of LvDaxx in vivo resulted in down-regulation of shrimp AMPs and reduction of WSSV copies in tissues. Furthermore, suppression of LvDaxx significantly decreased the mortality of WSSV-infected shrimps, but increased the mortality of Vibrio Parahaemolyticus-infected shrimps. Thus, these suggested that LvDaxx could play a role in the innate immunity against Vibrio parahaemolyticus in L. vannamei, while in the antiviral response, LvDaxx may be hijacked by WSSV and play a complex role in WSSV pathogenesis.
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