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利用杆状病毒表达系统在昆虫细胞中表达了完整的中国河北株丙型肝炎病毒（ＨＣＶ）结构蛋白。免疫印迹实验结果显示，表达产物中有一系列分子量不同、可以与ＨＣＶ抗体阳性病人血清反应的蛋白，表明结构蛋白被宿主细胞蛋白酶切割与加工，相应分别为２０ｋＤ的核心蛋白、３２ｋＤ糖基化的Ｅ１蛋白、４０ｋＤ的未糖化的Ｅ２蛋白和７０ｋＤ糖基化的Ｅ２蛋白，另有８０ｋＤ及１００ｋＤ的两组前体蛋白。利用表达产物检测慢性ＨＣＶ感染者血清，发现Ｅ２抗体检出率很高，而其中一部分核心抗体为阴性。免疫小鼠试验证明此蛋白可诱导特异性抗体产生
A complete Chinese hepatitis C virus (HCV) structural protein was expressed in insect cells using a baculovirus expression system. Western blotting results showed that a series of proteins with different molecular weights could react with the serum of HCV antibody-positive patients, indicating that the structural proteins were cut and processed by host cell proteases, corresponding to 20 kD core protein, 32 kD glycosylated E1 Protein, 40 kD of non-glycated E2 protein and 70 kD of glycosylated E2 protein, and another two sets of precursor proteins of 80 kD and 100 kD. Using the expression product to detect sera from patients with chronic HCV infection, the detection rate of E2 antibody was high, and some of the core antibodies were negative. Immunization of mice proved that this protein can induce specific antibody production