Molecular expression and enzymatic characterization of thioredoxin from the carcinogenic human liver fluke Opisthorchis viverrini |
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Authors: | Suttiprapa Sutas Matchimakul Pitchaya Loukas Alex Laha Thewarach Wongkham Sopit Kaewkes Sasithorn Brindley Paul J Sripa Banchob |
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Institution: | a Graduate School, Khon Kaen University, Khon Kaen 40002, Thailandb Tropical Disease Research Laboratory, Departments of Pathology, Khon Kaen University, Khon Kaen 40002, Thailandc Biochemistry, Khon Kaen University, Khon Kaen 40002, Thailandd Parasitology, Faculty of Medicine, Khon Kaen University, Khon Kaen 40002, Thailande Liver Fluke and Cholangiocarcinoma Research Center, Khon Kaen University, Khon Kaen 40002, Thailandf Queensland Tropical Health Alliance, James Cook University, Cairns, QLD 4878, Australiag Department of Microbiology, Immunology & Tropical Medicine, The George Washington University Medical Center, Washington, DC 20037, USA |
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Abstract: | The human liver fluke, Opisthorchis viverrini, induces inflammation of the hepatobiliary system. Despite being constantly exposed to inimical oxygen radicals released from inflammatory cells, the parasite survives for years. Defense against oxidative damage can be mediated through glutathione and/or thioredoxin utilizing systems. Here, we report the molecular expression and biochemical characterization of a thioredoxin (Trx) from O. viverrini. O. viverrini Trx cDNA encoded a polypeptide of 105 amino acid residues, of molecular mass 11.63 kDa. The predicted protein has similarity to previously characterized thioredoxins with 26-51% identity. Recombinant O. viverrini Trx (Ov-Trx-1) was expressed as soluble protein in E. coli. The recombinant protein showed insulin reduction activity and supported the enzymatic function of O. viverrini thioredoxin peroxidase. Expression of Ov-Trx-1 at mRNA and protein levels was observed in all obtainable developmental stages of the liver fluke. Ov-Trx-1 was also detected in excretory-secretory products released by adult O. viverrini. Immunohistochemistry, Ov-Trx-1 was expressed in nearly all parasite tissue excepted ovary and mature sperms. Interestingly, Ov-Trx-1 was observed in the infected biliary epithelium but not in normal bile ducts. These results suggest that Ov-Trx-1 is essential for the parasite throughout the life cycle. In the host-parasite interaction aspect, Ov-Trx-1 may support thioredoxin peroxidase in protecting the parasite against damage induced by reactive oxygen species from inflammation. |
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Keywords: | Liver fluke Opisthorchis viverrini Thioredoxin Redox system Antioxidant |
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