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Identification and biochemical characterization of two novel peroxiredoxins in a liver fluke, Clonorchis sinensis

Published online by Cambridge University Press:  22 July 2011

Y.-A. BAE ,
S.-H. KIM ,
E.-G. LEE ,
W.-M. SOHN  and
Y. KONG
Y.-A. BAE
Affiliation:
Department of Molecular Parasitology, Sungkyunkwan University School of Medicine, and Center for Molecular Medicine, Samsung Biomedical Research Center, Suwon 440-746, Korea
S.-H. KIM
Affiliation:
Department of Molecular Parasitology, Sungkyunkwan University School of Medicine, and Center for Molecular Medicine, Samsung Biomedical Research Center, Suwon 440-746, Korea
E.-G. LEE
Affiliation:
Department of Molecular Parasitology, Sungkyunkwan University School of Medicine, and Center for Molecular Medicine, Samsung Biomedical Research Center, Suwon 440-746, Korea
W.-M. SOHN
Affiliation:
Department of Parasitology and Institute of Health Sciences, Gyeongsang National University College of Medicine, Jinju 660-751, Korea
Y. KONG*
Affiliation:
Department of Molecular Parasitology, Sungkyunkwan University School of Medicine, and Center for Molecular Medicine, Samsung Biomedical Research Center, Suwon 440-746, Korea
*
*Corresponding author: Department of Molecular Parasitology, Sungkyunkwan University School of Medicine, 300 Cheoncheon-dong, Jangan-gu, Suwon 440-746, Korea. Tel: +82 31 299 6251. Fax: +82 31 299 6269. E-mail: [email protected]
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Summary

We identified 2 novel genes encoding different 2-Cys peroxiredoxins (PRxs), designated CsPRx2 and CsPRx3, in Clonorchis sinensis, which invades the human hepatobiliary tracts. The CsPRx2 gene expression was temporally increased along with the parasite's development and its protein product was detected in almost all parts of adult worms including subtegument, as well as excretory-secretory products. Conversely, CsPRx3 expression was temporally maintained at a basal level and largely restricted within interior parts of various tissues/organs. The recombinant forms of CsPRx proteins exhibited reducing activity against various hydroperoxides in the presence of either thioredoxin or glutathione (GSH) as a reducing equivalent, although they preferred H2O2 and GSH as a catalytic substrate and electron donor, respectively. A steady-state kinetic study demonstrated that the CsPRx proteins followed a saturable, Michaelis-Menten-type equation with the catalytic efficiencies (kcat/Km) ranging from 103 to 104 M−1 s−1, somewhat lower than those for other PRxs studied (104–105 M−1 s−1). The expression patterns and histological distributions specific to CsPRx2 and CsPRx3 might suggest different physiological functions of the antioxidant enzymes in protecting the worms against oxidative damage.

Keywords

Clonorchis sinensisantioxidant enzymeperoxiredoxinthioredoxin-dependent peroxidaseglutathione-dependent peroxidase
Type
Research Article
Information
Parasitology , Volume 138 , Issue 9 , August 2011 , pp. 1143 - 1153
Copyright
Copyright © Cambridge University Press 2011

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Supplementary material: File

Bae Supplementary Figure 1 Legend

Bae Supplementary Figure 1 Legend

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Bae Supplementary Table

Supplementary Table 1. Pairwise matrix of divergence rates among trematode PRx proteins based on the JTT model

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Bae Supplementary Figure 1

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