中文摘要：

对丙型肝炎病毒（HCV）截短型包膜糖蛋白E2-661基因进行原核表达和纯化。利用PCR法扩增出661bp的截短型HCVE2区基因片段，并将测序正确的E2-661基因克隆入原核表达载体pET28a中，转化大肠杆菌B121（DE3），经IPTG诱导表达后，通过SDS—PAGE和Western—blot对表达产物进行分析和鉴定。结果表明目的蛋白分子量约为35kDa，主要以包涵体形式大量存在。Western-blot结果显示目的蛋白与抗His标签单抗及HCV阳性血清均具有良好的反应原性。并通过镍离子亲和层析方法获得纯化的重组蛋白。以上结果为HCVE2功能的进一步研究奠定了基础。

英文摘要：

To construct a recombinant prokaryotic plasmid of truncated HCV E2 （E2-661） and observe its expression in E. coli, HCV E2-661 gene fragment was amplified by PCR. After verified by sequencing. It was inserted into the prokaryotic expression vector plasmid pET28a. The recombinant plasmid pET28a-E2-661 was then transformed into E. coil BL21 （DE3） to express the fusion protein induced with IPTG. The expression product was detected by SDS-PAGE and western-blot. The fusion protein mainly aggregated into the inclusion body. The results of western-blot showed that the expressed protein showed good reactivity to anti-His tag antibody and HCV positive serum. The protein E2-661 fused with His tag was purified by Ni-NTA resin column. The expression and purification of HCV E2-661 protein will be useful for further research on the function of envelope glycoprotein E2.