A novel scavenger receptor-cysteine-rich (SRCR) domain containing scavenger receptor identified from mollusk mediated PAMP recognition and binding

doi:10.1016/j.dci.2010.09.010

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	A novel scavenger receptor-cysteine-rich (SRCR) domain containing scavenger receptor identified from mollusk mediated PAMP recognition and binding
	Liu, Lin 1,2; Yang, Jialong 1,2; Qiu, Limei 1; Wang, Lingling 1; Zhang, Huan 1,2; Wang, Mengqiang1,2 ; Vinu, S. S.1; Song, Linsheng 1
刊名	DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY
	2011-02-01
卷号	35 期号:2 页码:227-239
关键词	Invertebrate Chlamys Farreri Innate Immunity Pattern Recognition Receptor Scavenger Receptor Srcr Domain
ISSN号	0145-305X
DOI	10.1016/j.dci.2010.09.010
文献子类	Article
英文摘要	Scavenger receptors (SRs) are significant endocytic receptors contributing to constant internal environment. SR-cysteine-rich (SRCR) domain-containing SR is the most important class of SRs which has been so far reported exclusively in mammals and birds. In the present study, a novel SRCR domain-containing SR (CfSR) was firstly identified from scallop Chlamys farreri. The full-length cDNA of CfSR was of 2639 bp encoding a polypeptide of 804 amino acids with a signal peptide, six SRCR domains, a UPAR-like domain and a ShK toxin-like domain. All the SRCR domains contain highly conserved six cysteine residues to form three pairs of intradomain disulfide, among which SRCR-D5 was assumed to participate in ligand-binding. An attachment site of sequence CTTPLCN was found in UPAR-like domain, indicating CfSR was an anchor protein. This prediction was confirmed by its localization on the outer surface of hemocytes with immunofluorescence assay. The mRNA expression of CfSR was up-regulated significantly by the stimulations of lipopolysaccharides, peptidoglycan and beta-glucan. A truncated CfSR (from V-456 to T-804) including SRCR-D5 was recombined and expressed in Escherichia coli, and the recombined protein displayed unique broad ligand-binding properties not only for acetylated low density lipoprotein (Ac-LDL) and dextran sulfate, but also for various pathogen associated molecular patterns, such as LPS, PGN, mannan and zymosan. All the results indicated that CfSR, the most primitive SR identified to date, was a versatile PRR involved in immune recognition, and the existence of functional SR might trace back to at least mollusk phylum. (C) 2010 Elsevier Ltd. All rights reserved.; Scavenger receptors (SRs) are significant endocytic receptors contributing to constant internal environment. SR-cysteine-rich (SRCR) domain-containing SR is the most important class of SRs which has been so far reported exclusively in mammals and birds. In the present study, a novel SRCR domain-containing SR (CfSR) was firstly identified from scallop Chlamys farreri. The full-length cDNA of CfSR was of 2639 bp encoding a polypeptide of 804 amino acids with a signal peptide, six SRCR domains, a UPAR-like domain and a ShK toxin-like domain. All the SRCR domains contain highly conserved six cysteine residues to form three pairs of intradomain disulfide, among which SRCR-D5 was assumed to participate in ligand-binding. An attachment site of sequence CTTPLCN was found in UPAR-like domain, indicating CfSR was an anchor protein. This prediction was confirmed by its localization on the outer surface of hemocytes with immunofluorescence assay. The mRNA expression of CfSR was up-regulated significantly by the stimulations of lipopolysaccharides, peptidoglycan and beta-glucan. A truncated CfSR (from V(456) to T(804)) including SRCR-D5 was recombined and expressed in Escherichia coil, and the recombined protein displayed unique broad ligand-binding properties not only for acetylated low density lipoprotein (Ac-LDL) and dextran sulfate, but also for various pathogen associated molecular patterns, such as LPS, PGN, mannan and zymosan. All the results indicated that CfSR, the most primitive SR identified to date, was a versatile PRR involved in immune recognition, and the existence of functional SR might trace back to at least mollusk phylum. (C) 2010 Elsevier Ltd. All rights reserved.
学科主题	Immunology ; Zoology
URL标识	查看原文
语种	英语
WOS记录号	WOS:000285127400009
公开日期	2012-07-03
内容类型	期刊论文
源URL	[http://ir.qdio.ac.cn/handle/337002/11758]
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, Key Lab Expt Marine Biol, Inst Oceanol, Qingdao 266071, Shandong, Peoples R China 2.Chinese Acad Sci, Grad Sch, Beijing 100049, Peoples R China
推荐引用方式 GB/T 7714	Liu, Lin,Yang, Jialong,Qiu, Limei,et al. A novel scavenger receptor-cysteine-rich (SRCR) domain containing scavenger receptor identified from mollusk mediated PAMP recognition and binding[J]. DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY,2011,35(2):227-239.
APA	Liu, Lin.,Yang, Jialong.,Qiu, Limei.,Wang, Lingling.,Zhang, Huan.,...&Song, Linsheng.(2011).A novel scavenger receptor-cysteine-rich (SRCR) domain containing scavenger receptor identified from mollusk mediated PAMP recognition and binding.DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY,35(2),227-239.
MLA	Liu, Lin,et al."A novel scavenger receptor-cysteine-rich (SRCR) domain containing scavenger receptor identified from mollusk mediated PAMP recognition and binding".DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY 35.2(2011):227-239.