Molecular cloning and characterization of a cyclophilin A homologue from Schistosoma japonicum

文献类型： 外文期刊

第一作者： Han, Hongxiao

作者： Han, Hongxiao;Xu, Jinjun;Tao, Jianping;Han, Hongxiao;Peng, Jinbiao;Hong, Yang;Fu, Zhiqiang;Lin, Jiaojiao;Peng, Jinbiao

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期刊名称：PARASITOLOGY RESEARCH （ 影响因子：2.289； 五年影响因子：2.403 ）

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收录情况： SCI

摘要： Cyclophilins belong to a group of proteins that have peptidyl-prolyl cis-trans isomerase activity and have been identified in all cell types and all organisms studied. In both prokaryotes and eukaryotes, they have been characterized as functional chaperones and involved in cell signaling. In the present study, Sj cyclophilin A (CyPA) was cloned, characterized, and subcloned into a prokaryotic expression vector to produce soluble recombinant rSjCyPA protein. qPCR analysis revealed that SjCyPA was expressed at each schistosome developmental stage tested, but reached its highest levels at days 7 and 13. In addition, the gene was also found to be significantly downregulated in adult worms from Microtus fortis. The SjCyPA protein was located on the subtegumentalmusculature of Schistosoma japonicum as determined by immunohistochemical staining analysis. Direct administration of recombinant SjCyPAtomice induced partial protective efficacy against subsequent schistosome infection. Length and width of adult worms and expression of SjCyPAwere significantly decreased in the immunized groups, at 42 days post-infection, indicating that immunizationwith recombinant SjCyPA may suppress the schistosomes development. rSjCyPA can also react with sera fromS. japonicum-infected rabbits at different time points. The data presented here suggest that SjCyPA may be an important molecule in the schistosome life-cycle and may be useful as a therapeutic target to treat schistosomiasis infection or as a potential diagnostic antigen.

分类号： R53

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