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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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