【摘 要】
：
来源于牛分枝杆菌的热休克蛋白65(Hsp65)在没有佐剂的情况下可作为载体分子将抗原表位递呈给免疫系统.热休克蛋白具有蛋白酶的催化活性,容易发生自溶而降解,这制约了基于Hsp6
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来源于牛分枝杆菌的热休克蛋白65(Hsp65)在没有佐剂的情况下可作为载体分子将抗原表位递呈给免疫系统.热休克蛋白具有蛋白酶的催化活性,容易发生自溶而降解,这制约了基于Hsp65疫苗的研究.该研究中,建立了纯化Hsp65及其融合蛋白Hsp65-6×P277(P277为来源于人热休克蛋白60的肽段,线性重复6次)的方法.Hsp65与Hsp65-6×P277以可溶形式表达于大肠杆菌.在低温及添加EDTA的条件下经细胞裂解、硫酸铵沉淀及阴离子交换树脂等纯化方法,可得到电泳纯的目的蛋白.用纯化的融合蛋白Hsp65-6×P277免疫小鼠,可激发机体产生强烈的免疫应答,该融合蛋白有希望作为免佐剂的糖尿病疫苗加以进一步研究开发.
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