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A novel serine protease with clip domain from scallop Chlamys farreri

文献类型： 外文期刊

作者： Zhu, Ling 1 ; Song, Linsheng 1 ; Mao, Yuze 3 ; Zhao, Jiangmin 1 ; Li, Chenghua 1 ; Xu, Wei 1 ;

作者机构： 1.Chinese Acad Sci, Inst Oceanol, Qingdao 266071, Peoples R China

2.Chinese Acad Sci, Key Lab Trop Marine Environm Dynam LED, S China Sea Inst Oceanog, Guangzhou 510301, Peoples R China

3.Chinese Acad Fishery Sci, Yellow Sea Fisheries Res Inst, Mariculture Ecol Div, Qingdao 266071, Peoples R China

关键词： Chlamys farreri;clip domain;immune response;mRNA expression;serine protease;tissue distribution

期刊名称：MOLECULAR BIOLOGY REPORTS （ 影响因子：2.316； 五年影响因子：2.357 ）

ISSN： 0301-4851

年卷期： 2008 年 35 卷 2 期

页码：

收录情况： SCI

摘要： The serine proteases with clip domain are involved in various innate immune functions in invertebrate such as antimicrobial activity, cell adhesion, pattern recognition and regulation of the prophenoloxidase system. A serine protease with clip-domain cDNA (Cf SP) was obtained by Expressed sequence taggings (ESTs) method and rapid amplification of cDNA ends (RACE). The Cf SP full-length cDNA was of 1,152 bp, including a 5'-terminal untranslated region (UTR) of 63 bp, a 3'-terminal UTR of 81 bp with a canonical polyadenylation signal sequence AATAAA and a poly(A) tail, and an open reading frame of 1,008 bp encoding a polypeptide of 336 amino acids with a putative signal peptide of 19 amino acids. The deduced amino acid sequence of Cf SP contained an amino-terminal clip domain with three disulfide bonds formed six conserved Cys residues, a carboxyl-terminal trypsin-like domain with the conserved His-Asp-Ser catalytic triad, and a low complexity linker sequence. The Cf SP was strongly expressed in hemocytes and the mRNA expression of Cf SP was up-regulated and increased 3.2-fold and 2.6-fold at 16 h after injection of Vibrio anguillarum and Micrococcus luteus. The results suggested that Cf SP gene might be involved in immune response of Gram-negative and Gram-positive microbial infection in scallop.

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