本文旨在获得纯化丙型肝炎病毒（HCV）核心蛋白（HCV-C）及抗HCV-C多克隆抗体，为深入研究HCV-C与肝细胞相互作用的分子机制奠定基础。首先以HCV1b亚型HC-J4-91全基因组质粒为模板，聚合酶链反应（PCR）扩增HCV-C基因，构建重组质粒pQE31-HCV-C。融合蛋白经原核表达、纯化后，免疫BALB/c小鼠，制备抗HCV-C多克隆抗体。利用酶联免疫吸附试验（ELISA）检测抗体效价，免疫印迹（Western blot）和间接免疫荧光染色鉴定抗体特异性。结果显示，表达HCV-C的原核表达质粒pQE31-HCV-C构建正确，获得相对分子质量（Mr）约22 000的纯化融合蛋白。ELISA检测重组蛋白免疫小鼠的抗血清效价达1:12 800。结果显示，自制的多克隆抗体能特异性识别HCV-C。本研究获得了纯度较好的、原核表达的HCV-C，并成功制备了抗HCV-C多克隆抗体，为深入研究HCV-C的致病机制提供了有实用价值的研究工具。

To investigate the interaction between hepatitis C virus core protein (HCV-C) and liver cells, purified HCV-C was obtained and polyclonal antibodies against HCV-C were prepared in the present study. The plasmid containing HC-J4-91 whole genome of HCV1b subtype was used as the template and the HCV-C gene was TA-cloned by polymerase chain reaction (PCR). The prokaryotic expression plasmid containing 6×His and HCV-C gene was constructed and named as pQE31-HCV-C. After expression in Escherichia coli and purification, the recombinant HCV-C was used to immunize BALB/c mice to obtain the antiserum. The titer and specificity of the antibody were determined by enzyme-linked immunosorbent assay (ELISA), Western blot and indirect immunofluorescence staining. The results demonstrated that the prokaryotic expression plasmid pQE31-HCV-C expressing a 22 000 fusion protein was successfully constructed. ELISA showed that antiserum against HCV-C from immunized mice had high antibody level, with titer at 1:12 800. Immunofluorescence staining and Western blot indicated that the antibody had good specificity and could recognize nature and unnatural HCV-C. It is concluded that the purified HCV-C protein and anti-HCV-C polyclonal antibodies obtained in this study might be useful for studying the molecular interaction mechanism between HCV-C and liver cells.