The galectin-3-binding protein of sCynoglossus emilaevis is a secreted protein of the innate immune system that binds a wide range of bacteria and is involved in host phagocytosis
文献类型：期刊论文
| 作者 | Chen, Cheng1,2; Chi, Heng1; Sun, Bo-guang1 ; Sun, Li1
|
| 刊名 | DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY
 |
| 出版日期 | 2013-04-01 |
| 卷号 | 39期号:4页码:399-408 |
| 关键词 | Galectin-3 binding protein Cynoglossus semilaevis Scavenger receptor Phagocytosis |
| ISSN号 | 0145-305X |
| 通讯作者 | Sun, L |
| 中文摘要 | Galectin-3 binding protein (G3BP) is a secreted glycoprotein that binds galectin-3 and is involved in various pathological conditions including cancer and viral infection. In fish, G3BP-like sequences have been identified in very few species and their biological properties are entirely unknown. In this work, we reported for the first time the identification and analysis of a teleost G3BP, CsG3BP, from half-smooth tongue sole (Cynoglossus semilaeyis). C5G3BP is composed of 565 amino acids and possesses a Scavenger Receptor Cysteine-rich (SRCR) domain, the latter containing six conserved cysteine residues that were predicted to form three intramolecular disulfide bridges. Expression of C5G3BP was detected in a wide range of tissues and upregulated by bacterial and megalocytivirus infection in a time-dependent manner. Immunoblot analysis detected CsG3BP in the culture medium of peripheral blood leukocytes (PBL) and in serum following bacterial stimulation. Purified recombinant C5G3BP (rC5G3BP) exhibited bacterial binding ability in a dose-dependent manner. In contrast, the mutant forms of C5G3BP that bear deletion of the SRCR domain or serine substitutions at three cysteine residues involved in disulfide bond formation lost the capacity of bacterial interaction. rCsG3BP displayed a certain substrate preference and bound more effectively to Gram-negative bacteria than to Gram-positive bacteria. Further study showed that when the CsG3BP produced by PBL was blocked by anti-rCsG3BP antibodies, the phagocytic activity of the cells was significantly reduced. Taken together, these results indicate that C5G3BP is a secreted protein that probably plays a role in innate immune defense by binding to bacterial cells via the SRCR domain and thereby facilitating host phagocytosis. (C) 2012 Elsevier Ltd. All rights reserved. |
| 英文摘要 | Galectin-3 binding protein (G3BP) is a secreted glycoprotein that binds galectin-3 and is involved in various pathological conditions including cancer and viral infection. In fish, G3BP-like sequences have been identified in very few species and their biological properties are entirely unknown. In this work, we reported for the first time the identification and analysis of a teleost G3BP, CsG3BP, from half-smooth tongue sole (Cynoglossus semilaeyis). C5G3BP is composed of 565 amino acids and possesses a Scavenger Receptor Cysteine-rich (SRCR) domain, the latter containing six conserved cysteine residues that were predicted to form three intramolecular disulfide bridges. Expression of C5G3BP was detected in a wide range of tissues and upregulated by bacterial and megalocytivirus infection in a time-dependent manner. Immunoblot analysis detected CsG3BP in the culture medium of peripheral blood leukocytes (PBL) and in serum following bacterial stimulation. Purified recombinant C5G3BP (rC5G3BP) exhibited bacterial binding ability in a dose-dependent manner. In contrast, the mutant forms of C5G3BP that bear deletion of the SRCR domain or serine substitutions at three cysteine residues involved in disulfide bond formation lost the capacity of bacterial interaction. rCsG3BP displayed a certain substrate preference and bound more effectively to Gram-negative bacteria than to Gram-positive bacteria. Further study showed that when the CsG3BP produced by PBL was blocked by anti-rCsG3BP antibodies, the phagocytic activity of the cells was significantly reduced. Taken together, these results indicate that C5G3BP is a secreted protein that probably plays a role in innate immune defense by binding to bacterial cells via the SRCR domain and thereby facilitating host phagocytosis. (C) 2012 Elsevier Ltd. All rights reserved. |
| WOS标题词 | Science & Technology ; Life Sciences & Biomedicine |
| 学科主题 | Immunology ; Zoology |
| 类目[WOS] | Immunology ; Zoology |
| 研究领域[WOS] | Immunology ; Zoology |
| 关键词[WOS] | CYSTEINE-RICH SUPERFAMILY ; CYNOGLOSSUS-SEMILAEVIS ; MAC-2-BINDING PROTEIN ; IMMUNOPROTECTIVE ANALYSIS ; VACCINE CANDIDATE ; BREAST-CANCER ; RECEPTOR ; IDENTIFICATION ; ANTIGEN ; EXPRESSION |
| 收录类别 | SCI |
| 原文出处 | 10.1016/j.dci.2012.10.008 |
| 语种 | 英语 |
| WOS记录号 | WOS:000317248900010 |
| 公开日期 | 2014-07-17 |
| 源URL | [http://ir.qdio.ac.cn/handle/337002/16647]  |
| 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 |
| 推荐引用方式 GB/T 7714 | Chen, Cheng,Chi, Heng,Sun, Bo-guang,et al. The galectin-3-binding protein of sCynoglossus emilaevis is a secreted protein of the innate immune system that binds a wide range of bacteria and is involved in host phagocytosis[J]. DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY,2013,39(4):399-408. |
| APA | Chen, Cheng,Chi, Heng,Sun, Bo-guang,&Sun, Li.(2013).The galectin-3-binding protein of sCynoglossus emilaevis is a secreted protein of the innate immune system that binds a wide range of bacteria and is involved in host phagocytosis.DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY,39(4),399-408. |
| MLA | Chen, Cheng,et al."The galectin-3-binding protein of sCynoglossus emilaevis is a secreted protein of the innate immune system that binds a wide range of bacteria and is involved in host phagocytosis".DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY 39.4(2013):399-408. |
入库方式： OAI收割
来源：海洋研究所
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