摘要
目的鉴定纯化的重组细粒棘球蚴热休克蛋白70(EgHSP70)的免疫学特性。方法对已构建的阳性表达菌EgHSP70/pGEX-6P-1进行大量诱导表达后纯化,用EgHSP70和HSP70/GST作抗原制剂分别免疫小鼠,制备抗血清,通过ELISA法和Western blot法对重组EgHSP70的免疫学特性进行鉴定。结果ELISA法检测结果表明,原头蚴、囊液等天然抗原均可被免疫小鼠血清识别,与对照组相比差异有统计学意义(P<0.05);Western blot显示免疫小鼠血清能够有效识别重组蛋白,同时重组EgHSP70也可被免疫兔血清识别。结论纯化后的重组蛋白EgHSP70具有较好的免疫原性和抗原性,可望作为包虫病疫苗候选分子,值得进一步深入研究。
Objective To identify the immunogencity of the purified Echinococcus granulosus heat shock protein 70.Methods The positive expression clone pGEX6p-1/HSP70 was induced by IPTG to produce sufficient recombinant fusion protein HSP70/GST.The purified proteins were injected into mice.The immunogenicity of the specific antibody and its level were identified by Western blot and ELISA.Results With Western blot and ELISA detected,the results showed that crude proteins including protoscoles and cystic fluid,could be recognized by its HSP70immunized mouse except that the purified protein could be recognized by the sera from the rabbits infected with Eg.Conclusion The purified protein HSP70 has higher immunogenicity and may be a new vaccination candidate.
出处
《宁夏医学院学报》
2007年第5期454-456,459,共4页
Journal of Ningxia Medical College
基金
国家自然科学基金项目(项目编号:30260105)
宁夏自然科学基金资助项目:批准号NZ0540
宁夏卫生厅科技重点计划项目资助
