肺炎链球菌SP2159基因编码的岩藻胶蛋白相关蛋白(FRP)的聚糖结合谱

Albert M. Wu , Tanuja Singh , Yung Liang Chen , Kimberly M. Anderson , Su Chen Li , Yu Teh Li
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引用次数: 2

摘要

在大肠杆菌中表达了由肺炎链球菌SP2159基因编码的功能未知的重组岩藻集素相关蛋白(FRP)。在本研究中,通过酶联凝集素吸附和抑制实验检测了其聚糖识别表位及其结合能力。结果表明,FRP与人血型ABH和l-Fucα1→2-活性糖基发生强烈反应,并以多价(超)形式发生反应。当用质量相对效价表示时,FRP与聚l- fuc α1→糖基的结合亲和力比单l- fuc α1→糖基的结合亲和力高5.0 × 105倍。FRP的这种独特的结合特性可以作为区分l-Fucα1→2复合物形式和其他形式的糖基的特殊工具。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

Glycan binding profile of a fucolectin-related protein (FRP) encoded by the SP2159 gene of Streptococcus pneumoniae

Glycan binding profile of a fucolectin-related protein (FRP) encoded by the SP2159 gene of Streptococcus pneumoniae

Glycan binding profile of a fucolectin-related protein (FRP) encoded by the SP2159 gene of Streptococcus pneumoniae

Glycan binding profile of a fucolectin-related protein (FRP) encoded by the SP2159 gene of Streptococcus pneumoniae

The recombinant fucolectin-related protein (FRP) of unknown function, encoded by the SP2159 gene of Streptococcus pneumoniae, was expressed in E. coli. In this study, its glycan-recognition epitopes and their binding potencies were examined by enzyme-linked lectinosorbent and inhibition assays. The results indicate that FRP reacted strongly with human blood group ABH and l-Fucα1→2-active glycotopes and in their polyvalent (super) forms. When expressed by mass relative potency, the binding affinities of FRP to poly-l-Fucα1→glycotopes were about 5.0 × 105 folds higher than that of the mono-l-Fucα1→glycotope form. This unique binding property of FRP can be used as a special tool to differentiate complex forms of l-Fucα1→2 and other forms of glycotopes.

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