Characterization of the antioxidant enzyme, thioredoxin peroxidase, from the carcinogenic human liver fluke, Opisthorchis viverrini

Suttiprapa, Sutas, Loukas, Alex, Laha, Thewarach, Wongkham, Sopit, Kaewkes, Sasithorn, Gaze, Soraya, Brindley, Paul J. and Sripa, Banchob (2008) Characterization of the antioxidant enzyme, thioredoxin peroxidase, from the carcinogenic human liver fluke, Opisthorchis viverrini. Molecular and Biochemical Parasitology, 160 2: 116-122. doi:10.1016/j.molbiopara.2008.04.010


Author Suttiprapa, Sutas
Loukas, Alex
Laha, Thewarach
Wongkham, Sopit
Kaewkes, Sasithorn
Gaze, Soraya
Brindley, Paul J.
Sripa, Banchob
Title Characterization of the antioxidant enzyme, thioredoxin peroxidase, from the carcinogenic human liver fluke, Opisthorchis viverrini
Formatted title
Characterization of the antioxidant enzyme, thioredoxin peroxidase, from the carcinogenic human liver fluke, Opisthorchis viverrini
Journal name Molecular and Biochemical Parasitology   Check publisher's open access policy
ISSN 0166-6851
1872-9428
Publication date 2008-08
Sub-type Article (original research)
DOI 10.1016/j.molbiopara.2008.04.010
Volume 160
Issue 2
Start page 116
End page 122
Total pages 7
Place of publication Amsterdam, Netherlands
Publisher Elsevier
Language eng
Formatted 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 many years. The mechanisms by which it avoids oxidative damage are unknown. In this study, thioredoxin peroxidase (TPx), a member of the peroxiredoxin superfamily, was cloned from an O. viverrini cDNA library. O. viverrini TPx cDNA encoded a polypeptide of 212 amino acid residues, of molecular mass 23.57 kDa. The putative amino acid sequence shared 60–70% identity with TPXs from other helminths and from mammals, and phylogenetic analysis revealed a close relationship between TPxs from O. viverrini and other trematodes. Recombinant O. viverrini TPx was expressed as soluble protein in Escherichia coli. The recombinant protein dimerized, and its antioxidant activity was deduced by observing protection of nicking of supercoiled plasmid DNA by hydroxyl radicals. Antiserum raised against O. viverrini TPx recognized native proteins from egg, metacercaria and adult developmental stages of the liver fluke and excretory–secretory products released by adult O. viverrini. Immunolocalization studies revealed ubiquitous expression of TPx in O. viverrini organs and tissues. TPx was also detected in bile fluid and bile duct epithelial cells surrounding the flukes 2 weeks after infection of hamsters with O. viverrini. In addition, TPx was observed in the secondary (small) bile ducts where flukes cannot reach due to their large size. These results suggested that O. viverrini TPx plays a significant role in protecting the parasite against damage induced by reactive oxygen species from inflammation.
Keyword Liver fluke
Opisthorchis viverrini
Peroxiredoxin
Thioredoxin peroxidase
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: ERA 2012 Admin Only
School of Public Health Publications
 
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Created: Mon, 31 Oct 2011, 11:02:52 EST by Geraldine Fitzgerald on behalf of School of Public Health