深海热液区管状蠕虫Ridgeia piscesae中Ricin B-lectin型结构域基因的克隆与表达

作为一种重要的模式识别因子,凝集素在多个领域中均有着广泛的应用价值,因此,开发和利用新型凝集素将具有重要意义.本研究以生活在深海热液区极端环境条件下的管状蠕虫Ridgeia piscesae为材料,首次从管状蠕虫中克隆获得Ricin B-lectin基因rgal.序列分析表明,RGAL与已知序列的相似性较低,其含有2个Ricin B-lectin型结构域,并且该结构域具有该家族所特有的β-三叶草形三维结构.多方面的分析结果显示RGAL可能是一个新颖的凝集素蛋白.对RGAL进行了原核重组表达,并对其复性条件进行了摸索优化,成功获得了其可溶性表达产物,为后续RGAL的生物活性分析奠定了坚实的基础.

Clone and expression of the gene with a Ricin B-lectin domain of the tubeworm,Ridgeia piscesae,from the hydrothermal vent

Lectin,as an important family of pattern recognition receptors,has been applied widely in various fields.Therefore,development and utilization of new lectins are of great significance.In this study,a Ricin B-lectin gene rgal was first cloned from the tubeworm Ridgeia piscesae,which lives around the hydrothermal vent.Sequence analysis revealed that RGAL had low homology with the known sequence.However,it contained two homologous β-trefoil fold typical of the Ricin B-lectin domains.These results suggested that RGAL might be a novel lectin.Furthermore,the RGAL was cloned and recombinant expressed and the soluble proteins were obtained.The study will establish a basis for further study on properties and functions of the RGAL.