A fibrinogen-related protein from bay scallop Argopecten irradians involved in innate immunity as pattern recognition receptor

doi:10.1016/j.fsi.2008.07.019

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	A fibrinogen-related protein from bay scallop Argopecten irradians involved in innate immunity as pattern recognition receptor
	Zhang, Huan 1,2; Wang, Lingling 1; Song, Linsheng 1; Song, Xiaoyan 3; Wang, Bo 1,2; Mu, Changkao 1,2; Zhang, Ying 1,2
	2009
发表期刊	FISH & SHELLFISH IMMUNOLOGY
ISSN	1050-4648
卷号	26 期号:1 页码:56-64
文章类型	Article
摘要	The family of fibrinogen-related proteins (FREPs) is a group of proteins with fibrinogen-like domains. Many members of this family play important roles as pattern recognition receptors in innate immune responses. The cDNA of bay scallop Argopecten irradians FREP (designated as AiFREP) was cloned by rapid amplification of cDNA ends (RACE) method based on the expressed sequence tag (EST). The full-length cDNA of AiFREP was of 990 bp. The open reading frame encoded a polypeptide of 251 amino acids, including a signal sequence and a 213 amino acids fibrinogen-like domain. The fibrinogen-like domain of AiFREP was highly similar to those of mammalian ficolins and other FREPs. The temporal expression of AiFREP mRNA in hemolymph was examined by fluorescent quantitative real-time PCR. The mRNA level of scallops challenged by Listonella anguillarum was significantly up-regulated, peaked to 9.39-fold at 9 h after stimulation, then dropped back to 4.37-fold at 12 h, while there was no significant change in the Micrococcus luteus challenged group in all periods of treatment. The function of AiFREP was investigated by recombination and expression of the cDNA fragment encoding its mature peptide in Escherichia coli Rosetta gami (DE3). The recombinant AiFREP (rAiFREP) agglutinated chicken erythrocytes and human A, B, O-type erythrocytes. The agglutinating activities were calcium-dependent and could be inhibited by acetyl group-containing carbohydrates. rAiFREP also agglutinated Gram-negative bacteria E. coli JM109, L anguillarum and Gram-positive bacteria M. luteus in the presence of calcium ions. These results collectively suggested that AiFREP functions as a pattern recognition receptor in the immune response of bay scallop and contributed to nonself recognition in invertebrates, which would also provide clues for elucidating the evolution of the lectin pathway of the complement system. (C) 2008 Elsevier Ltd. All rights reserved.; The family of fibrinogen-related proteins (FREPs) is a group of proteins with fibrinogen-like domains. Many members of this family play important roles as pattern recognition receptors in innate immune responses. The cDNA of bay scallop Argopecten irradians FREP (designated as AiFREP) was cloned by rapid amplification of cDNA ends (RACE) method based on the expressed sequence tag (EST). The full-length cDNA of AiFREP was of 990 bp. The open reading frame encoded a polypeptide of 251 amino acids, including a signal sequence and a 213 amino acids fibrinogen-like domain. The fibrinogen-like domain of AiFREP was highly similar to those of mammalian ficolins and other FREPs. The temporal expression of AiFREP mRNA in hemolymph was examined by fluorescent quantitative real-time PCR. The mRNA level of scallops challenged by Listonella anguillarum was significantly up-regulated, peaked to 9.39-fold at 9 h after stimulation, then dropped back to 4.37-fold at 12 h, while there was no significant change in the Micrococcus luteus challenged group in all periods of treatment. The function of AiFREP was investigated by recombination and expression of the cDNA fragment encoding its mature peptide in Escherichia coli Rosetta gami (DE3). The recombinant AiFREP (rAiFREP) agglutinated chicken erythrocytes and human A, B, O-type erythrocytes. The agglutinating activities were calcium-dependent and could be inhibited by acetyl group-containing carbohydrates. rAiFREP also agglutinated Gram-negative bacteria E. coli JM109, L anguillarum and Gram-positive bacteria M. luteus in the presence of calcium ions. These results collectively suggested that AiFREP functions as a pattern recognition receptor in the immune response of bay scallop and contributed to nonself recognition in invertebrates, which would also provide clues for elucidating the evolution of the lectin pathway of the complement system. (C) 2008 Elsevier Ltd. All rights reserved.
关键词	Argopecten Irradiant Fibrinogen-related Protein Innate Immunity Pattern Recognition Receptor Hemagglutinating Activity Bacterial Agglutinating Activity
学科领域	Fisheries ; Immunology ; Marine & Freshwater Biology ; Veterinary Sciences
DOI	10.1016/j.fsi.2008.07.019
URL	查看原文
收录类别	SCI
语种	英语
WOS记录号	WOS:000264015700008
引用统计	被引频次：79[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/337002/3066
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, Shandong, Peoples R China 2.Chinese Acad Sci, Grad Sch, Beijing 100049, Peoples R China 3.NW A&F Univ, Yangling 712100, Shaanxi, 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	Zhang, Huan,Wang, Lingling,Song, Linsheng,et al. A fibrinogen-related protein from bay scallop Argopecten irradians involved in innate immunity as pattern recognition receptor[J]. FISH & SHELLFISH IMMUNOLOGY,2009,26(1):56-64.
APA	Zhang, Huan.,Wang, Lingling.,Song, Linsheng.,Song, Xiaoyan.,Wang, Bo.,...&Zhang, Ying.(2009).A fibrinogen-related protein from bay scallop Argopecten irradians involved in innate immunity as pattern recognition receptor.FISH & SHELLFISH IMMUNOLOGY,26(1),56-64.
MLA	Zhang, Huan,et al."A fibrinogen-related protein from bay scallop Argopecten irradians involved in innate immunity as pattern recognition receptor".FISH & SHELLFISH IMMUNOLOGY 26.1(2009):56-64.

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