A novel serine protease with clip domain from scallop Chlamys farreri

doi:10.1007/s11033-007-9078-2

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	A novel serine protease with clip domain from scallop Chlamys farreri
	Zhu, Ling 1,2; Song, Linsheng 1; Mao, Yuze 3; Zhao, Jiangmin 1; Li, Chenghua 1; Xu, Wei 1
	2008-06-01
发表期刊	MOLECULAR BIOLOGY REPORTS
ISSN	0301-4851
卷号	35 期号:2 页码:257-264
文章类型	Article
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.; 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.
关键词	Chlamys Farreri Clip Domain Immune Response Mrna Expression Serine Protease Tissue Distribution
学科领域	Biochemistry & Molecular Biology
DOI	10.1007/s11033-007-9078-2
URL	查看原文
收录类别	SCI
语种	英语
WOS记录号	WOS:000256082300024
引用统计	被引频次：20[WOS] [WOS记录] [WOS相关记录]
文献类型	期刊论文
条目标识符	http://ir.qdio.ac.cn/handle/337002/5770
专题	实验海洋生物学重点实验室
作者单位	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
第一作者单位	中国科学院海洋研究所
推荐引用方式 GB/T 7714	Zhu, Ling,Song, Linsheng,Mao, Yuze,et al. A novel serine protease with clip domain from scallop Chlamys farreri[J]. MOLECULAR BIOLOGY REPORTS,2008,35(2):257-264.
APA	Zhu, Ling,Song, Linsheng,Mao, Yuze,Zhao, Jiangmin,Li, Chenghua,&Xu, Wei.(2008).A novel serine protease with clip domain from scallop Chlamys farreri.MOLECULAR BIOLOGY REPORTS,35(2),257-264.
MLA	Zhu, Ling,et al."A novel serine protease with clip domain from scallop Chlamys farreri".MOLECULAR BIOLOGY REPORTS 35.2(2008):257-264.

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