重组人β趋化因子RANTES基因融合表达产物活性分析

Fused Expression and Activity Analysis of Recombinant Human β-Chemokine RANTES Gene

为研制基于病毒受体的抗艾滋病毒感染基因药物 ,将重组人 β趋化因子RANTES基因导入大肠杆菌中表达谷胱甘肽S 转移酶 (GST) RANTES融合蛋白 ,并回收携带末端延伸肽 (TEP)的RANTES修饰蛋白 .荧光免疫化学分析表明 ,2种非天然RANTES蛋白均显示对人外周血淋巴细胞的结合活性 .暗示在细胞表面可能已发生RANTES与CCR5之间的相互作用 .2种修饰RANTES蛋白都能使人外周血细胞的过氧化物酶活性显著升高 ,提示这 2个人造蛋白可能仍存在对淋巴细胞的趋化性诱导 .

To prepare a viral receptor based genetic medicine against infection of AIDS virus, the recombinant human β chemokine RANTES gene was introduced into E.coli for expressing a glutathione S transferase (GST) RANTES fusion protein, and recovering a terminal extension peptide (TEP) containing modified RANTES protein. The fluorescent immunochemical analysis showed that both non natural RANTES proteins demonstrated binding activities to human peripheral blood lymphocytes, implying an interaction between RANTES and CCR5 on the cell surface might have occurred. Furthermore, two forms of modified RANTES proteins were able to enhance the peroxidase activity of human peripheral blood cells, suggesting that chemotaxis induction for lymphosytes in these two artificial proteins could be still present.