Molecular expression and enzymatic characterization of thioredoxin from the carcinogenic human liver fluke Opisthorchis viverrini

被引：17

作者：

Suttiprapa, Sutas ^{[2
,3
,5
]}

Matchimakul, Pitchaya ^{[2
]}

Loukas, Alex ^{[4
]}

Laha, Thewarach

Wongkham, Sopit ^{[3
]}

Kaewkes, Sasithorn ^{[3
]}

Brindley, Paul J. ^{[5
]}

Sripa, Banchob ^{[1
,3
]}

机构：

[1] Khon Kaen Univ, Fac Med, Dept Pathol, Trop Dis Res Lab, Khon Kaen 40002, Thailand

[2] Khon Kaen Univ, Grad Sch, Khon Kaen 40002, Thailand

[3] Khon Kaen Univ, Liver Fluke & Cholangiocarcinoma Res Ctr, Khon Kaen 40002, Thailand

[4] James Cook Univ, Queensland Trop Hlth Alliance, Cairns, Qld 4878, Australia

[5] George Washington Univ, Med Ctr, Dept Microbiol Immunol & Trop Med, Washington, DC 20037 USA

来源：

PARASITOLOGY INTERNATIONAL | 2012年 / 61卷 / 01期

基金：

英国医学研究理事会;

关键词：

Liver fluke; Opisthorchis viverrini; Thioredoxin; Redox system; Antioxidant; FUNCTIONAL-CHARACTERIZATION; HETEROLOGOUS EXPRESSION; FASCIOLA-HEPATICA; CELLS; PEROXIDASE; MECHANISM; THAILAND;

D O I：

10.1016/j.parint.2011.06.018

中图分类号：

R38 [医学寄生虫学]; Q [生物科学];

学科分类号：

07 ; 0710 ; 09 ; 100103 ;

摘要：

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. (C) 2011 Elsevier Ireland Ltd. All rights reserved.

引用

页码：101 / 106

页数：6

共 26 条

[1] Molecular and enzymatic characterisation of Schistosoma mansoni thioredoxin [J].