Molecular cloning and characterization of a thioester-containing protein from Zhikong scallop Chlamys farreri

doi:10.1016/j.molimm.2007.03.008

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	Molecular cloning and characterization of a thioester-containing protein from Zhikong scallop Chlamys farreri
	Zhang, Huan ; Song, Linsheng ; Li, Chenghua ; Zhao, Jianmin ; Wang, Hao ; Gao, Qiang ; Xu, Wei
刊名	MOLECULAR IMMUNOLOGY
	2007-07-01
卷号	44 期号:14 页码:3492-3500
关键词	Chlamys Farreri Thioester-containing Protein Gene Cloning Complement Evolution Rt-pcr
ISSN号	0161-5890
DOI	10.1016/j.molimm.2007.03.008
文献子类	Article
英文摘要	Thioester-containing proteins are a family of proteins characterized by the unique intrachain beta-cysteinyl-gamma-glutamyl thioester, which play important roles in innate immune responses. The cDNA of Zhikong scallop Chlamys farreri thioester-containing protein (designated as CfTEP) was cloned by expressed sequence tag (EST) and rapid amplification of cDNA ends (RACE) approaches. The full-length cDNA of CfTEP was of 4616 bp, consisting of a 5 '-terminal untranslated region (UTR) of 30 bp and a 3 ' UTR of 140 bp with a polyadenylation signal sequence AATAAA and a poly(A) tail. The CfTEP cDNA encoded a polypeptide of 1481 amino acids with the theoretical isoelectric point of 5.98 and the predicted molecular weight of 161.4 kDa. The deduced amino acid sequence of CfTEP contained the canonical thioester motif GCGEQ, nine potential N-glycosylation sites and a C-terminal distinctive cysteine signature. It also contained a presumed catalytic histidine and proteolytic cleavage sites that were similar to C3 molecules. The high similarity of CfTEP with the thioester-containing proteins in other organisms, such as the TEPs from insects, the complement component C3, C4, C5 and the protease inhibitor alpha(2)-macroglobulin indicated that CfTEP should be a member of TEP family. The phylogenetic analysis revealed that CfTEP was closely related to TEPs from mollusc, nematodes and insects, and they formed a separate branch apart from the branches of complements factors and alpha(2)-macroglobulins. The spatial expression of CfTEP transcripts in healthy and bacterial challenged scallops was examined by semi-quantitative RT-PCR. The CfTEP transcripts were mainly detected in the tissues of hepatopancreas and gonad, and remarkably up-regulated by Microbial challenge, which suggested that CfTEP was a constitutive and inducible acute-phase protein involved in immune defense. These results provided new insights into the role of CfTEP in scallop immune responses, as well as the evolutionary origin of this important, widespread and functionally diversified family of proteins. (c) 2007 Published by Elsevier Ltd.; Thioester-containing proteins are a family of proteins characterized by the unique intrachain beta-cysteinyl-gamma-glutamyl thioester, which play important roles in innate immune responses. The cDNA of Zhikong scallop Chlamys farreri thioester-containing protein (designated as CfTEP) was cloned by expressed sequence tag (EST) and rapid amplification of cDNA ends (RACE) approaches. The full-length cDNA of CfTEP was of 4616 bp, consisting of a 5 '-terminal untranslated region (UTR) of 30 bp and a 3 ' UTR of 140 bp with a polyadenylation signal sequence AATAAA and a poly(A) tail. The CfTEP cDNA encoded a polypeptide of 1481 amino acids with the theoretical isoelectric point of 5.98 and the predicted molecular weight of 161.4 kDa. The deduced amino acid sequence of CfTEP contained the canonical thioester motif GCGEQ, nine potential N-glycosylation sites and a C-terminal distinctive cysteine signature. It also contained a presumed catalytic histidine and proteolytic cleavage sites that were similar to C3 molecules. The high similarity of CfTEP with the thioester-containing proteins in other organisms, such as the TEPs from insects, the complement component C3, C4, C5 and the protease inhibitor alpha(2)-macroglobulin indicated that CfTEP should be a member of TEP family. The phylogenetic analysis revealed that CfTEP was closely related to TEPs from mollusc, nematodes and insects, and they formed a separate branch apart from the branches of complements factors and alpha(2)-macroglobulins. The spatial expression of CfTEP transcripts in healthy and bacterial challenged scallops was examined by semi-quantitative RT-PCR. The CfTEP transcripts were mainly detected in the tissues of hepatopancreas and gonad, and remarkably up-regulated by Microbial challenge, which suggested that CfTEP was a constitutive and inducible acute-phase protein involved in immune defense. These results provided new insights into the role of CfTEP in scallop immune responses, as well as the evolutionary origin of this important, widespread and functionally diversified family of proteins. (c) 2007 Published by Elsevier Ltd.
学科主题	Biochemistry & Molecular Biology ; Immunology
URL标识	查看原文
语种	英语
WOS记录号	WOS:000247683300005
公开日期	2010-12-24
内容类型	期刊论文
源URL	[http://ir.qdio.ac.cn/handle/337002/5737]
专题	海洋研究所_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, Grad Sch, Beijing 100049, Peoples R China
推荐引用方式 GB/T 7714	Zhang, Huan,Song, Linsheng,Li, Chenghua,et al. Molecular cloning and characterization of a thioester-containing protein from Zhikong scallop Chlamys farreri[J]. MOLECULAR IMMUNOLOGY,2007,44(14):3492-3500.
APA	Zhang, Huan.,Song, Linsheng.,Li, Chenghua.,Zhao, Jianmin.,Wang, Hao.,...&Xu, Wei.(2007).Molecular cloning and characterization of a thioester-containing protein from Zhikong scallop Chlamys farreri.MOLECULAR IMMUNOLOGY,44(14),3492-3500.
MLA	Zhang, Huan,et al."Molecular cloning and characterization of a thioester-containing protein from Zhikong scallop Chlamys farreri".MOLECULAR IMMUNOLOGY 44.14(2007):3492-3500.