F-type lectin from the sea bass (Dicentrarchus labrax): Purification, cDNA cloning, tissue expression and localization, and opsonic activity
F-type lectin from the sea bass (Dicentrarchus labrax): Purification, cDNA cloning, tissue expression and localization, and opsonic activity
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DOI：
10.1016/j.fsi.2009.01.004
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发表时间：
2009-08-01
影响因子：
4.7
通讯作者：
Cammarata, M.
中科院分区：
文献类型：
--
作者：
Salerno, G.;Parisi, M. G.;Cammarata, M.
最近描述的来自欧洲鳗鱼（Anguilla anguilla）和条纹鲈（Morone saxatilis）的岩藻糖结合凝集素的生物化学和结构方面导致鉴定出一个新的凝集素家族（“F型”凝集素），其特征在于独特的序列基序和特征性结构折叠。 F型折叠不仅与该凝集素家族的其他成员共享，而且还与从原核生物到脊椎动物等明显不相关的蛋白质共享。在这里，我们描述了从鲈鱼 (Dicentrarchus labrax) 血清中分离的 F 型凝集素 (DlFBL) 的纯化、生化和分子特性以及调理活性。 DlFBL 具有两个串联排列的碳水化合物识别结构域，显示 F 型序列基序。原位杂交和免疫组织化学分析表明，DlFBL 特异性表达并定位于肝细胞和肠细胞。相对于未暴露的对照，福尔马林灭活的大肠杆菌暴露于 DlFBL 增强了拉布拉克斯腹膜巨噬细胞的吞噬作用，表明 DlFBL 可能在血浆和肠粘液中充当调理素。 (C) 2009 Elsevier Ltd. 保留所有权利。
Recently described biochemical and structural aspects of fucose-binding lectins from the European eel (Anguilla anguilla) and striped bass (Morone saxatilis) led to the identification of a novel lectin family ("F-type" lectins) characterized by a unique sequence motif and a characteristic structural fold. The F-type fold is shared not only with other members of this lectin family, but also with apparently unrelated proteins ranging from prokaryotes to vertebrates. Here we describe the purification, biochemical and molecular properties, and the opsonic activity of an F-type lectin (DlFBL) isolated from sea bass (Dicentrarchus labrax) serum. DlFBL exhibits two tandemly arranged carbohydrate-recognition domains that display the F-type sequence motif In situ hybridization and immunohistochemical analysis revealed that DlFBL is specifically expressed and localized in hepatocytes and intestinal cells. Exposure of formalin-killed Escherichia coli to DlFBL enhanced their phagocytosis by D. labrax peritoneal macrophages relative to the unexposed controls, suggesting that DlFBL may function as an opsonin in plasma and intestinal mucus. (C) 2009 Elsevier Ltd. All rights reserved.