The cDNA cloning and mRNA expression of cytoplasmic Cu, Zn superoxide dismutase (SOD) gene in scallop Chlamys farreri

被引:87
作者
Ni, Duojiao
Song, Linsheng
Gao, Qiang
Wu, Longtao
Yu, Yundong
Zhao, Jianmin
Qiu, Limei
Zhang, Huan
Shi, Fangfang
机构
[1] Chinese Acad Sci, Inst Oceanol, Qingdao 266071, Peoples R China
[2] Chinese Acad Sci, Grad Sch, Beijing 100039, Peoples R China
基金
中国国家自然科学基金;
关键词
scallop; Chlamys farreri; reactive oxygen species (ROS); superoxide dismutase (SOD); innate immunity; mRNA expression;
D O I
10.1016/j.fsi.2007.04.008
中图分类号
S9 [水产、渔业];
学科分类号
0908 ;
摘要
Cu, Zn superoxide dismutases (SODs) are rnetalloenzymes that represent one important line of defence against reactive oxygen species (ROS). A cytoplasmic Cu. Zn SOD cDNA sequence was cloned from scallop Chlamys farreri by the homology-based cloning technique. The full-length cDNA of scallop cytoplasmic Cu, Zn SOD (designated CfSOD) was 1022 bp with a 459 bp open reading frame encoding a polypeptide of 153 amino acids. The predicted amino acid sequence of CfSOD shared high identity with cytoplasmic Cu. Zn SOD in molluscs, insects, mammals and other animals, such as cytoplasmic Cu, Zn SOD in oyster Crassostrea sostrea gigas (CAD42722), mosquito Aedes aegypti (ABF18094), and cow Bos taurus (XP_584414). A quantitative reverse transcriptase real-time PCR (qRT-PCR) assay was developed to assess the mRNA expression of CfSOD in different tissues and the temporal expression of CfSOD in scallop challenged with Listonella anguillarum, Micrococcus luteus and Candida lipolytica respectively. Higher-level mRNA expression of CfSOD was detected in the tissues of haemocytes, gill filaments and kidney. The expression of CfSOD dropped in the first 8-16 h and then recovered after challenge with L. anguillarum and M. litteus, but no change was induced by the C. lipolytica challenge. The results indicated that CfSOD was a constitutive and inducible acute-phase protein, and could play an important role in the immune responses against L. anguillarum and M. luteus infection. (C) 2007 Elsevier Ltd. All rights reserved.
引用
收藏
页码:1032 / 1042
页数:11
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