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Expression, characterization and crystal structure of thioredoxin from Schistosoma japonicum

  • YONGDONG LI (a1) (a2) (a3), PAN LI (a2), YUN PENG (a2), QUNFENG WU (a1) (a2) (a3), FUYAN HUANG (a2), XIANG LIU (a2), XUN LI (a2), HUI ZHOU (a2), DAOYI GUO (a2), DASHUANG SHI (a2) (a4), XIAO-NONG ZHOU (a1) (a3) and XIAOLIN FAN (a2)...


Schistosoma japonicum, a human blood fluke, causes a parasitic disease affecting millions of people in Asia. Thioredoxin–glutathione system of S. japonicum plays a critical role in maintaining the redox balance in parasite, which is a potential target for development of novel antischistosomal agents. Here we cloned the gene of S. japonicum thioredoxin (SjTrx), expressed and purified the recombinant SjTrx in Escherichia coli. Functional assay shows that SjTrx catalyses the dithiothreitol (DTT) reduction of insulin disulphide bonds. The coupling assay of SjTrx with its endogenous reductase, thioredoxin glutathione reductase from S. japonicum (SjTGR), supports its biological function to maintain the redox homeostasis in the cell. Furthermore, the crystal structure of SjTrx in the oxidized state was determined at 2·0 Å resolution, revealing a typical architecture of thioredoxin fold. The structural information of SjTrx provides us important clues for understanding the maintenance function of redox homeostasis in S. japonicum and pathogenesis of this chronic disease.


Corresponding author

* Corresponding authors. Key Laboratory on Biology of Parasite and Vector, Ministry of Health, and WHO Collaborating Center for Malaria, Schistosomiasis and Filariasis, Shanghai 200025, People's Republic of China, Key Laboratory of Organo-Pharmaceutical Chemistry, Jiangxi Province, Chemistry and Chemical Engineering College, Gannan Normal University, Ganzhou 341000, People's Republic of China. E-mail: and


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