目的构建含沙眼衣原体外膜蛋白2(Omp2)抗原编码基因的表达质粒,在E.coli中表达 Omp2。方法通过PCR方法扩增D型沙眼衣原体omp2基因片段,克隆于表达载体pQE30,转化大肠杆菌M15感受态细胞,IPTG诱导表达,用SDS-PAGE及Western blot进行Omp2表达的鉴定。结果经酶切分析和DNA序列鉴定,构建了pQE30/omp2重组表达质粒;获得了相对分子质量(Mr)约为60 × 103的融合蛋白,能与抗-6聚组氨酸单克隆抗体发生特异性反应。结论利用原核表达载体,成功地表达了Omp2,为进一步开展其免疫学功能的研究奠定了基础。 Objective To construct an expression plasmid encoding Chlamydia trachomatis outer protein 2 (Omp2) antigen and express Omp2 in E. coli. Methods The omp2 gene fragment of Chlamydia trachomatis type D was amplified by PCR and cloned into expression vector pQE30. The recombinant plasmid was transformed into E. coli M15 and induced by IPTG. The expression of Omp2 was identified by SDS-PAGE and Western blot. Results The recombinant plasmid pQE30 / omp2 was constructed by enzyme digestion analysis and DNA sequence identification. The fusion protein with molecular weight of about 60 × 103 was obtained, which was specific to anti-6 polyhistidine monoclonal antibody Sexual response. Conclusion The prokaryotic expression vector Omp2 was successfully expressed, which laid the foundation for the further study of its immunological function.