Prokaryotic expression of TsCL-1 gene from Taenia solium metacestode.

【Objective】In order to lay a basis for researching the role of cysteine protease(CP)in the relationship between Cysticercus cellulosae and its host,the study explored the characteristics of the recombinant protein expressed prokaryotically.【Method】The recombinant plasmid pGEX-4T-TsCL-1 was transformed into and prokaryotically expressed in E.coli BL21.The expressed products were purified by using GST sepharose FF affinity chromatography.The proteolytic activity of CP was assayed by using zymography.【Result】SDS-PAGE analysis showed that the molecular weight of recombinant protein was about 61 ku,which corresponded well to the predicted size from the primary sequence of the gene.The purity of the purified protein was more than 90%.The analysis of hydrolysis activity and inhibition experiments showed that CP possessed a hydrolytic activity,and the hydrolytic activity can be specifically inhibited by E-64. 【Conclusion】The target protein was successfully expressed,and the protein has obviously hydrolysis activity.The hydrolytic activity of this protein can be inhibited by E-64.