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本文构建并表达了旋毛虫热休克蛋白70（Ts－Hsp70）与排泄分泌抗原Ts87的融合蛋白，并对融合蛋白进行纯化和免疫学鉴定。本研究采用限制性内切酶EcoRⅠ酶切位点将目的基因Ts－Hsp70与Ts87相连接，插入pET28－a （＋）质粒，转入大肠埃希菌BL21（DE3）中诱导表达、纯化，获得的融合蛋白rTs－Hsp70－Ts87用Western blot的方法鉴定。经PCR、酶切鉴定、测序分析，结果显示，目的基因片段大小为2721 bp，构建的重组质粒与预期相符。经IPTG诱导表达，通过镍离子柱层析纯化复性后得到可溶的融合蛋白rTs－Hsp70－Ts87，其相对分子质量约为100 kDa； Western blot结果显示，该蛋白可被抗His标签单抗、 rTs－Hsp70免疫血清、 rTs87免疫血清识别。以上结果表明，本研究成功构建并表达了融合蛋白rTs－Hsp70－Ts87，为进一步研究rTs－Hsp70－Ts87的免疫保护性，开发新的有效抗旋毛虫病的疫苗奠定基础。“,”To construct and express the fusion protein that combines Trichinella spiralis heat shock protein 70 with excretory-secretory antigen Ts87, restriction enzyme EcoRⅠ site was applied to fuse Ts-Hsp70 with Ts87.The target genes were inserted into plasmid pET28-a ( +), and transformed into E.coli.BL21 (DE3).After expression and purification, the fusion protein rTs-Hsp70-Ts87 was characterized by SDS-PAGE and Western blot.The results showed that the fusion gene was 2 721 bp.The results of PCR, enzyme digestion and sequencing analysis showed that the recombinant plasmid was affirmed to be successfully constructed.The fusion protein rTs-Hsp70-Ts87 was expressed with IPTG induction and purified by Ni-affinity chromatography and refolded.The results of SDS-PAGE and Western blot indicated that molecular weight of the protein is about 100 kDa, and it could be recognized by anti His-tag monoclonal antibody, anti-rTs-Hsp70 immune serum and anti-rTs87 immune serum.In conclusion, T.spiralis recombinant fusion protein rTs-Hsp70-Ts87 was constructed and expressed successfully, which had laid the groundwork for further research.