目的研究丙型肝炎病毒（ｈｅｐａｔｉｔｉｓ Ｃ ｖｉｒｕｓ，ＨＣＶ）不同长度Ｃ蛋白片段在大肠杆菌中的表达和纯化及其抗原性。方法应用核酸及蛋白分析软件对Ｃ蛋白的抗原决定簇预测分析，以ＰＣＲ方法扩增３段长度分别为２０１ｂｐ、４０２ｂｐ及５９１ｂｐ的Ｃ基因片段，通过基因体外重组技术克隆到ｐＧＥＸ－３Ｘ表达质粒中，用所获重组蛋白免疫ＢＡＬＢ／ Ｃ鼠并应用ＥＬＩＳＡ法对免疫动物系列稀释血清进行抗体测定和分析。结果 ＰＧＥＸ－３Ｘ表达质粒转化 ＢＬ２１（ＤＥ３），通过诱导、表达的 Ｃ２０１及 Ｃ４０２蛋白分子量分别为 ３．１×１０４及３．９×１０４的融台蛋白，以包涵体形式存在表达细胞内，而全Ｃ基因Ｃ５９１则未能有效地表达出相应蛋白。Ｃ４０２融合蛋白与丙型肝炎病人血清发生强特异性反应，而Ｃ２０１片段反应较弱。ＥＬＩＳＡ 法检测重组的Ｃ４０２蛋白免疫的ＢＡＬＢ／Ｃ鼠血清有明显的抗－ＨＣＶ核心抗体产生。结论确定ＨＣＶ Ｃ区主要抗原决定簇的基因片断对临床诊断试剂和ＨＣＶ基因疫苗的研制具有一定的意义。 Objective To study the expression, purification and antigenicity of different length C protein fragments of hepatitis C virus (HCV) in Escherichia coli. Methods The predicted protein C epitopes were predicted by nucleic acid and protein analysis software. Three C gene fragments of 201bp, 402bp and 591bp in length were amplified by PCR and cloned into the pGEX-3X expression plasmid by gene in vitro recombination BALB / C mice were immunized with the obtained recombinant protein and the serum of the immunized animals was subjected to antibody assay and analysis by ELISA. Results The PGEX-3X expression plasmid was transformed into BL21 (DE3). The induced molecular weights of C201 and C402 were 3.1 × 104 and 3.9 × 104, respectively, and expressed in inclusion bodies The whole C gene C591 failed to effectively express the corresponding protein. C402 fusion protein and hepatitis C patients with strong specificity of the reaction, and C201 fragment reaction is weak. The recombinant C402 protein immunized BALB / C mouse serum showed significant anti-HCV core antibody production by ELISA. Conclusion It is of some significance to determine the gene fragment of the major epitope of HCV C region for the development of clinical diagnostic reagents and HCV gene vaccine.