目的 :在大肠杆菌中表达SARS病毒S2与硫氧还原蛋白 (Trx)的融合蛋白 ,并对其进行血清学鉴定。方法 :克隆编码SARS病毒S2蛋白的基因 ,并在原核表达系统中表达了 6×His S2硫氧还原融合蛋白。用Westernblot分析纯化Trx S2融合蛋白 ,分别与 6份SARS流行前的正常人血清和 6份SARS患者恢复期血清的反应性。结果 :Westernblot分析表明 ,6份SARS患者的恢复期血清均能识别Trx S2融合蛋白 ,且在Mr为 76× 10 3 附近出现特异性的结合带 ;而 6份SARS流行前的正常人血清则不与Trx S2融合蛋白起反应。结论 :本研究获得了纯化的SARS病毒Trx S2融合蛋白 ,它可与SARS患者的恢复期血清产生特异性结合反应 ,为研究SARS病毒感染宿主细胞的过程和制备针对SARS病毒的重组疫苗提供了条件。 Objective: To express the fusion protein of SARS virus S2 and thioredoxin (Trx) in Escherichia coli and to identify the fusion protein. Methods: The gene encoding SARS virus S2 protein was cloned and expressed in prokaryotic expression system as 6 × His S2 thioredoxin fusion protein. The purified Trx S2 fusion protein was analyzed by Western blotting, and was respectively associated with convalescent sera of 6 SARS patients and 6 normal subjects before SARS epidemic. Results: Westernblot analysis showed that the convalescent sera of six SARS patients recognized the Trx S2 fusion protein and showed a specific binding band around Mr = 76 × 10 3, while the normal human serum before the six SARS epidemic was not Reacts with Trx S2 fusion protein. Conclusion: The purified Trx S2 fusion protein of SARS virus was obtained in this study. It can produce specific binding reaction with convalescent sera of patients with SARS, which provides the conditions for studying the process of SARS virus infecting host cells and preparing recombinant vaccines against SARS virus .