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A novel scavenger receptor-cysteine-rich (SRCR) domain containing scavenger receptor identified from mollusk mediated PAMP recognition and binding
Liu, Lin1,2; Yang, Jialong1,2; Qiu, Limei1; Wang, Lingling1; Zhang, Huan1,2; Wang, Mengqiang1,2; Vinu, S. S.1; Song, Linsheng1
2011-02-01
发表期刊DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY
ISSN0145-305X
卷号35期号:2页码:227-239
文章类型Article
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.
关键词Invertebrate Chlamys Farreri Innate Immunity Pattern Recognition Receptor Scavenger Receptor Srcr Domain
学科领域Immunology ; Zoology
DOI10.1016/j.dci.2010.09.010
URL查看原文
收录类别SCI
语种英语
WOS记录号WOS:000285127400009
引用统计
被引频次:42[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/337002/11757
专题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
第一作者单位中国科学院海洋研究所
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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.
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