人免疫缺陷病毒I型 p24gag 基因的重组与表达

High Level Expression of p24 Protein of Human Immunodeficiency Virus Type 1 in E.coli

将编码人Ｉ型免疫缺陷病毒（ＨＩＶ－１）衣壳蛋白的ｐ２４ｇａｇ基因片段，克隆到原核表达载体ｐＥＴ－１７ｂ的Ｔ７噬菌体启动子下游，构建成了重组表达质粒ｐＥＴ２４，并使ｐ２４ｇａｇ基因片段在大肠杆菌ＢＬ２１（ＤＥ３）中高效表达，产物为３０ｋＤａ的ｓ１９－ｐ２４融合蛋白，表达量占菌体总蛋白的３８．４％。重组ｐ２４蛋白均与抗ｐ２４单克隆抗体及ＨＩＶ－１阳性血清发生特异性反应，具有较好的抗原性。

A plasmid vector pET24, containing the p24 gag gene fragment encoding the casid protein(p24) of human immunodeficiency virus type 1(HIV 1) under the control of the bacteriophage T7 promoter, was constructed, which highly expressed a 30kDa protein of s10 p24 that spaned 284 amino acid residues. The fusion protein was produced at a level of approximately 38.4% of the total cellular protein in Escherchia coli BL21(DE3) containing pET24. Western blot indicated that the recombinant protein could be recognized by anti p24 monoclonal antibody. It is useful for preparation of specific entibody, and diagnostic and prognostic uses.