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利用基因工程重组技术获得了绿色荧光蛋白（ｇｆｐ）基因与ＨＣＶ核心蛋白（ｃｏｒｅ）基因的嵌合体，并在大肠杆菌中高效表达了４８ｋＤａ的融合蛋白，经ＤｏｔＥＬＩＳＡ和Ｗｅｓｔｅｒｎｂｌｏｔ免疫活性分析证实，融合蛋白仍具有ｃｏｒｅ抗原的三个免疫活性部位，同时用荧光显微镜观察并用荧光光度计测定了大肠杆菌表达的融合蛋白的荧光光谱，结果证实，我们在大肠杆菌中表达的ＧＦＰｃｏｒｅ融合蛋白既能发射易于检测的绿色荧光，又具有ＨＣＶ核心蛋白的抗原活性，实现了用绿色荧光蛋白等分子标记抗原，为免疫诊断新方法的建立，打下了理论基础。
The chimeric gene of green fluorescent protein (gfp) gene and HCV core gene were obtained by genetic engineering recombination technology and the fusion protein of 48kDa was highly expressed in E. coli. The results of DotELISA and Western blot showed that the fusion protein was highly expressed in E.coli, The fusion protein still possesses three immunologically active sites of the core antigen. Fluorescence microscopy was also used to observe the fluorescence spectra of the fusion proteins expressed by E. coli. The results confirmed that the GFP-c fusion protein we expressed in E. coli Can emit easily detectable green fluorescence, but also has HCV core protein antigen activity, and has realized the use of molecular markers such as green fluorescent protein antigen for the establishment of a new immunodiagnostic method, laying a theoretical foundation.