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
文献类型：期刊论文
| 作者 | Qiu, Reng1,2; Sun, Bo-guang1 ; Li, Jun1,3; Liu, Xiao1; Sun, Li1
|
| 刊名 | FISH & SHELLFISH IMMUNOLOGY
 |
| 出版日期 | 2013-03-01 |
| 卷号 | 34期号:3页码:810-818 |
| 关键词 | Scavenger receptor Sciaenops ocellatus Pattern recognition receptor |
| ISSN号 | 1050-4648 |
| 通讯作者 | Sun, L |
| 中文摘要 | 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. |
| 英文摘要 | 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. |
| WOS标题词 | Science & Technology ; Life Sciences & Biomedicine |
| 学科主题 | Fisheries ; Immunology ; Marine & Freshwater Biology ; Veterinary Sciences |
| 类目[WOS] | Fisheries ; Immunology ; Marine & Freshwater Biology ; Veterinary Sciences |
| 研究领域[WOS] | Fisheries ; Immunology ; Marine & Freshwater Biology ; Veterinary Sciences |
| 关键词[WOS] | HOST-DEFENSE ; IMMUNOPROTECTIVE ANALYSIS ; SCOPHTHALMUS-MAXIMUS ; MACROPHAGE RECEPTOR ; VACCINE CANDIDATE ; IMMUNE DEFENSE ; IN-VITRO ; MARCO ; BINDING ; INFECTION |
| 收录类别 | SCI |
| 原文出处 | 10.1016/j.fsi.2012.12.016 |
| 语种 | 英语 |
| WOS记录号 | WOS:000316523300009 |
| 公开日期 | 2014-07-17 |
| 源URL | [http://ir.qdio.ac.cn/handle/337002/16587]  |
| 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, 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 |
| 推荐引用方式 GB/T 7714 | 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.(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. |
入库方式： OAI收割
来源：海洋研究所
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