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目的 :探讨幽门螺杆菌热休克蛋白A与尿素酶B融合蛋白的免疫生物学活性。方法 :采用亲和层析、离子交换和凝胶过滤对幽门螺杆菌热休克蛋白A与尿素酶B融合蛋白进行初步纯化 ,用粗纯化蛋白对小鼠进行免疫 ,然后分析其免疫活性。结果 :采用亲和层析或离子交换和凝胶过滤后 ,融合蛋白的纯度分别可达到 6 5 .6 %和90 .2 %。该融合蛋白可诱导小鼠产生抗幽门螺杆菌的胃肠黏液IgA和血清IgG抗体 ,并促使免疫小鼠脾脏T淋巴细胞CD4+ CD8+ 比值的增加。结论 :重组热休克蛋白A与尿素酶B融合蛋白可以诱导在未来免疫预防中起积极作用的免疫应答反应
Objective: To investigate the immunological biological activity of Helicobacter pylori heat shock protein A and urease B fusion protein. Methods: The fusion proteins of Helicobacter pylori heat shock protein A and urease B were preliminarily purified by affinity chromatography, ion exchange and gel filtration. The crude protein was used to immunize mice and the immunological activity was analyzed. Results: The purity of the fusion proteins reached 65.6% and 90.2%, respectively, by affinity chromatography or ion exchange and gel filtration. The fusion protein can induce mice to produce anti-Helicobacter pylori IgA and serum IgG antibodies, and promote immune T lymphocytes in mice with an increase of CD4 + CD8 + ratio. CONCLUSIONS: Recombinant heat shock protein A and urease B fusion proteins can induce an immune response that plays an active role in future immunoprophylaxis