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

doi:10.1016/j.dci.2012.10.008

IOCAS-IR > 实验海洋生物学重点实验室

	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
	Chen, Cheng 1,2; Chi, Heng 1; Sun, Bo-guang1 ; Sun, Li 1; Sun, L
	2013-04-01
发表期刊	DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY
ISSN	0145-305X
卷号	39 期号:4 页码:399-408
文章类型	Article
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.; 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.
关键词	Galectin-3 Binding Protein Cynoglossus Semilaevis Scavenger Receptor Phagocytosis
学科领域	Immunology ; Zoology
DOI	10.1016/j.dci.2012.10.008
URL	查看原文
收录类别	SCI
语种	英语
WOS研究方向	Immunology ; Zoology
WOS类目	Immunology ; Zoology
WOS记录号	WOS:000317248900010
WOS关键词	CYSTEINE-RICH SUPERFAMILY ; CYNOGLOSSUS-SEMILAEVIS ; MAC-2-BINDING PROTEIN ; IMMUNOPROTECTIVE ANALYSIS ; VACCINE CANDIDATE ; BREAST-CANCER ; RECEPTOR ; IDENTIFICATION ; ANTIGEN ; EXPRESSION
WOS标题词	Science & Technology ; Life Sciences & Biomedicine
引用统计	被引频次：29[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/337002/16647
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
第一作者单位	实验海洋生物学重点实验室
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,&Sun, L.(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.

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