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Identification and characterization of a cell surface scavenger receptor cysteine-rich protein of Sciaenops ocellatus: Bacterial interaction and its dependence on the conserved structural features of the SRCR domain
Qiu, Reng1,2; Sun, Bo-guang1; Li, Jun1,3; Liu, Xiao1; Sun, Li1; Sun, L
2013-03-01
发表期刊FISH & SHELLFISH IMMUNOLOGY
ISSN1050-4648
卷号34期号:3页码:810-818
文章类型Article
摘要The scavenger receptor cysteine-rich (SRCR) proteins are secreted or membrane-bound receptors with one or multiple SRCR domains. Members of the SRCR superfamily are known to have diverse functions that include pathogen recognition and immunoregulation. In teleost, although protein sequences with SRCR structure have been identified in some species, very little functional investigation has been carried out. In this study, we identified and characterized a teleost SRCR protein from red drum Sciaenops ocellatus. The protein was named S. ocellatus SRCR1 (SoSRCRP1). SoSRCRP1 is 410-residue in length and was predicted to be a transmembrane protein, with the extracellular region containing a collagen triple helix repeat and a SRCR domain. The SRCR domain has six conserved cysteines, of which, 038 and 099, C351 and C409, and C379 and 089 were predicted to form three disulfide bonds. SoSRCRP1 expression was detected mainly in immune-relevant tissues and upregulated by bacterial and viral infection. In head kidney leukocytes, bacterial infection stimulated the expression of SoSRCRP1, and the expressed SoSRCRP1 was localized on cell surface. Recombinant SoSRCRP1 (rSoSRCRP1) corresponding to the SRCR domain was purified from Escherichia coli and found to be able to bind Gram-negative and Gram-positive bacteria. To examine the structure function relationship of SoSRCRP1, the mutant proteins SoSRCRP1M1, SoSRCRP1M2, SoSRCRP1M3, and SoSRCRP1M4 were created, which bear C351S and C409S, C338S, C379S, and R325A mutations respectively. Compared to rSoSRCRP1, all mutants were significantly reduced in the ability of bacterial interaction, with the highest reduction observed with SoSRCRP1M4. Taken together, these results indicate that SoSRCRP1 is a cell surface-localized SRCR protein that binds bacterial ligands in a manner that depends on the conserved structural features of the SRCR domain. 2012 Elsevier Ltd. All rights reserved.; The scavenger receptor cysteine-rich (SRCR) proteins are secreted or membrane-bound receptors with one or multiple SRCR domains. Members of the SRCR superfamily are known to have diverse functions that include pathogen recognition and immunoregulation. In teleost, although protein sequences with SRCR structure have been identified in some species, very little functional investigation has been carried out. In this study, we identified and characterized a teleost SRCR protein from red drum Sciaenops ocellatus. The protein was named S. ocellatus SRCR1 (SoSRCRP1). SoSRCRP1 is 410-residue in length and was predicted to be a transmembrane protein, with the extracellular region containing a collagen triple helix repeat and a SRCR domain. The SRCR domain has six conserved cysteines, of which, 038 and 099, C351 and C409, and C379 and 089 were predicted to form three disulfide bonds. SoSRCRP1 expression was detected mainly in immune-relevant tissues and upregulated by bacterial and viral infection. In head kidney leukocytes, bacterial infection stimulated the expression of SoSRCRP1, and the expressed SoSRCRP1 was localized on cell surface. Recombinant SoSRCRP1 (rSoSRCRP1) corresponding to the SRCR domain was purified from Escherichia coli and found to be able to bind Gram-negative and Gram-positive bacteria. To examine the structure function relationship of SoSRCRP1, the mutant proteins SoSRCRP1M1, SoSRCRP1M2, SoSRCRP1M3, and SoSRCRP1M4 were created, which bear C351S and C409S, C338S, C379S, and R325A mutations respectively. Compared to rSoSRCRP1, all mutants were significantly reduced in the ability of bacterial interaction, with the highest reduction observed with SoSRCRP1M4. Taken together, these results indicate that SoSRCRP1 is a cell surface-localized SRCR protein that binds bacterial ligands in a manner that depends on the conserved structural features of the SRCR domain. 2012 Elsevier Ltd. All rights reserved.
关键词Scavenger Receptor Sciaenops Ocellatus Pattern Recognition Receptor
学科领域Fisheries ; Immunology ; Marine & Freshwater Biology ; Veterinary Sciences
DOI10.1016/j.fsi.2012.12.016
URL查看原文
收录类别SCI
语种英语
WOS研究方向Fisheries ; Immunology ; Marine & Freshwater Biology ; Veterinary Sciences
WOS类目Fisheries ; Immunology ; Marine & Freshwater Biology ; Veterinary Sciences
WOS记录号WOS:000316523300009
WOS关键词HOST-DEFENSE ; IMMUNOPROTECTIVE ANALYSIS ; SCOPHTHALMUS-MAXIMUS ; MACROPHAGE RECEPTOR ; VACCINE CANDIDATE ; IMMUNE DEFENSE ; IN-VITRO ; MARCO ; BINDING ; INFECTION
WOS标题词Science & Technology ; Life Sciences & Biomedicine
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被引频次:15[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/337002/16587
专题实验海洋生物学重点实验室
通讯作者Sun, L
作者单位1.Chinese Acad Sci, Inst Oceanol, Key Lab Expt Marine Biol, Qingdao 266071, Peoples R China
2.Chinese Acad Sci, Grad Univ, Beijing 100049, Peoples R China
3.Lake Super State Univ, Sch Biol Sci, Sault Ste Marie, MI USA
第一作者单位实验海洋生物学重点实验室
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Qiu, Reng,Sun, Bo-guang,Li, Jun,et al. Identification and characterization of a cell surface scavenger receptor cysteine-rich protein of Sciaenops ocellatus: Bacterial interaction and its dependence on the conserved structural features of the SRCR domain[J]. FISH & SHELLFISH IMMUNOLOGY,2013,34(3):810-818.
APA Qiu, Reng,Sun, Bo-guang,Li, Jun,Liu, Xiao,Sun, Li,&Sun, L.(2013).Identification and characterization of a cell surface scavenger receptor cysteine-rich protein of Sciaenops ocellatus: Bacterial interaction and its dependence on the conserved structural features of the SRCR domain.FISH & SHELLFISH IMMUNOLOGY,34(3),810-818.
MLA Qiu, Reng,et al."Identification and characterization of a cell surface scavenger receptor cysteine-rich protein of Sciaenops ocellatus: Bacterial interaction and its dependence on the conserved structural features of the SRCR domain".FISH & SHELLFISH IMMUNOLOGY 34.3(2013):810-818.
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