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为了增强胆固醇酯转移蛋白(CETP)羧基末端的26肽B细胞抗原表位的免疫原性,以大肠杆菌L-门冬酰胺酶II(AnsB)为载体,通过引入2个强的辅助T细胞表位,构建了融合基因AnsB-TTP-PADRE-CET-PC,并在大肠杆菌BL-21(DE3)表达,经过硫酸铵沉淀、DEAE 52纤维素阴离子交换层析、分子筛凝胶过滤层析,最终得到单一电泳条带纯度的目的蛋白。纯化的融合多肽疫苗免疫新西兰大白兔可诱导产生高水平持续存在的抗CETP抗体,从而抑制了CETP酶活力,显著抑制了兔主动脉斑粥样硬化斑的形成和发展。该融合蛋白有希望作为抗动脉粥样硬化疫苗进一步研究开发。
In order to enhance the immunogenicity of carboxyl-terminal 26 peptide B cell epitopes of cholesteryl ester transfer protein (CETP), Escherichia coli L-asparaginase II (AnsB) was used as a vector and two strong helper T cell tables The fusion gene AnsB-TTP-PADRE-CET-PC was constructed and expressed in E. coli BL-21 (DE3). After ammonium sulfate precipitation, DEAE 52 cellulose anion exchange chromatography and molecular sieve gel filtration chromatography, Get a single electrophoresis band purity of the target protein. The purified fusion polypeptide vaccine can induce high level of anti-CETP antibody in New Zealand white rabbits, which can inhibit the activity of CETP enzyme and significantly inhibit the formation and development of aortic plaque in rabbits. The fusion protein is promising for further research and development as an anti-atherosclerotic vaccine.