Molecular characterization, immune response against white spot syndrome virus infection of peroxiredoxin 4 in Fenneropenaeus chinensis and its antioxidant activity

文献类型： 外文期刊

第一作者： Zhang, Qingli

作者： Zhang, Qingli;Huang, Jie;Liu, Shuang;Liu, Qinghui;Liang, Gaofeng;Li, Fuhua;Wei, Jiankai;Xiang, Jianhai

作者机构：

关键词： Peroxiredoxin (Prx);White spot syndrome virus (WSSV) infection;Recombinant protein;Antioxidant activity

期刊名称：FISH & SHELLFISH IMMUNOLOGY （ 影响因子：4.581； 五年影响因子：4.851 ）

ISSN： 1050-4648

年卷期： 2014 年 37 卷 1 期

页码：

收录情况： SCI

摘要： Peroxiredoxins (Prx) are a family of antioxidant proteins and perform important functions in intracellular signal transduction. Here, we report a Prx gene from Chinese shrimp Fenneropenaeus chinensis. The full-length cDNA of FcPrx gene contained an open reading frame of 735 bp encoding a polypeptide of 275 amino acids. The molecular mass of the deduced amino acid of FcPrx is 27445.43 Da with an estimated pI of 5.71. Sequence comparison showed that the FcPrx shares high identities with Prx IVs and it was named FcPrx4. A real-Time PCR (qRT-PCR) assay was developed to assess the mRNA expression of FcPrx4 in different tissues and temporal expression in hemocytes and hepatopancreas of E chinensis challenged by white spot syndrome virus (WSSV). Transcripts of FcPrx4 can be detected in all tissues examined. The expression of FcPrx4 showed significant up-regulation in shrimp hemocytes and hepatopancreas after artificial infection with WSSV. A fusion protein containing FcPrx4 was produced in vitro and was confirmed by Matrix-assisted laser desorption ionization mass spectrometry (MALDI-MS) assay. And activity analysis indicated that the recombinant FcPrx4 proteins can reduce H2O2 in the presence of dithiothreitol. (C) 2014 Elsevier Ltd. All rights reserved.

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