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Characterization of a Thioredoxin-1 Gene from Taenia Solium and Its Encoding Product

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Journal Biomed Res Int
Publisher Wiley
Date 2015 Jun 20
PMID 26090410
Citations 3
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Abstract

Taenia solium thioredoxin-1 gene (TsTrx-1) has a length of 771 bp with three exons and two introns. The core promoter gene presents two putative stress transcription factor binding sites, one putative TATA box, and a transcription start site (TSS). TsTrx-1 mRNA is expressed higher in larvae than in adult. This gene encodes a protein of 107 amino acids that presents the Trx active site (CGPC), the classical secondary structure of the thioredoxin fold, and the highest degree of identity with the Echinococcus granulosus Trx. A recombinant TsTrx-1 (rTsTrx-1) was produced in Escherichia coli with redox activity. Optimal activity for rTsTrx-1 was at pH 6.5 in the range of 15 to 25°C. The enzyme conserved activity for 3 h and lost it in 24 h at 37°C. rTsTrx-1 lost 50% activity after 1 h and lost activity completely in 24 h at temperatures higher than 55°C. Best storage temperature for rTsTrx-1 was at -70°C. It was inhibited by high concentrations of H₂O₂ and methylglyoxal (MG), but it was inhibited neither by NaCl nor by anti-rTsTrx-1 rabbit antibodies that strongly recognized a ~12 kDa band in extracts from several parasites. These TsTrx-1 properties open the opportunity to study its role in relationship T. solium-hosts.

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Cloning, expression, purification, and kinetic characterization of mitochondrial thioredoxin (TsTrx2), cytosolic thioredoxin (TsTrx1), and glutaredoxin (TsGrx1) from Taenia solium.

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Molecular Cloning of a cDNA Encoding for Taenia solium TATA-Box Binding Protein 1 (TsTBP1) and Study of Its Interactions with the TATA-Box of Actin 5 and Typical 2-Cys Peroxiredoxin Genes.

Rodriguez-Lima O, Garcia-Gutierrez P, Jimenez L, Zarain-Herzberg A, Lazzarini R, Landa A PLoS One. 2015; 10(11):e0141818.

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References
1.
Chae H, Robison K, Poole L, Church G, Storz G, Rhee S . Cloning and sequencing of thiol-specific antioxidant from mammalian brain: alkyl hydroperoxide reductase and thiol-specific antioxidant define a large family of antioxidant enzymes. Proc Natl Acad Sci U S A. 1994; 91(15):7017-21. PMC: 44329. DOI: 10.1073/pnas.91.15.7017. View

2.
Rendon J, Del Arenal I, Guevara-Flores A, Uribe A, Plancarte A, Mendoza-Hernandez G . Purification, characterization and kinetic properties of the multifunctional thioredoxin-glutathione reductase from Taenia crassiceps metacestode (cysticerci). Mol Biochem Parasitol. 2003; 133(1):61-9. DOI: 10.1016/j.molbiopara.2003.09.003. View

3.
Mai B, Breeden L . Xbp1, a stress-induced transcriptional repressor of the Saccharomyces cerevisiae Swi4/Mbp1 family. Mol Cell Biol. 1997; 17(11):6491-501. PMC: 232502. DOI: 10.1128/MCB.17.11.6491. View

4.
Molina-Lopez J, Jimenez L, Ochoa-Sanchez A, Landa A . Molecular cloning and characterization of a 2-Cys peroxiredoxin from Taenia solium. J Parasitol. 2006; 92(4):796-802. DOI: 10.1645/GE-754R.1. View

5.
Vaca-Paniagua F, Parra-Unda R, Landa A . Characterization of one typical 2-Cys peroxiredoxin gene of Taenia solium and Taenia crassiceps. Parasitol Res. 2009; 105(3):781-7. DOI: 10.1007/s00436-009-1461-6. View