Purification and characterization of Taenia crassiceps cysticerci thioredoxin: insight into thioredoxin-glutathione-reductase (TGR) substrate recognition

Martínez-González, José de Jesús; Guevara-Flores, Alberto; Rendón, Juan L.; Sosa‐Peinado, Alejandro; Mena, Irene Patricia del Arenal

doi:10.1016/j.parint.2014.12.004

Cited by 6 publications

(3 citation statements)

References 80 publications

(96 reference statements)

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“…Kinetic constants of TcTGR were determined using TsTrx as a substrate with the following results: K m = 41.5 µM and k cat /K m = 1.2 × 10 6 M −1 s −1 (Table S1); despite having different K m , the catalytic efficiency values were comparable to those reported previously [43] and those reported for TsTGR and the recombinant TsTrx [38]. Additionally, the comparison of the TsTGR gene (ID: TsM_000506200) of the T. solium genome submitted in WormBase Parisite database (GENOME ID: PRJNA170813) and the TcTGR gene (ID: JAKROA010000003.1) submitted in the GenBank database (GENOME ID: GCA_023375655.1.)…”

Section: Kinetic Analysis Of Tctgrsupporting

confidence: 75%

A Physiological Approach to Explore How Thioredoxin–Glutathione Reductase (TGR) and Peroxiredoxin (Prx) Eliminate H2O2 in Cysticerci of Taenia

Guevara-Flores,

Nava-Balderas,

de Jesús Martínez-González

et al. 2024

Antioxidants

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Peroxiredoxins (Prxs) and glutathione peroxidases (GPxs) are the main enzymes of the thiol-dependent antioxidant systems responsible for reducing the H2O2 produced via aerobic metabolism or parasitic organisms by the host organism. These antioxidant systems maintain a proper redox state in cells. The cysticerci of Taenia crassiceps tolerate millimolar concentrations of this oxidant. To understand the role played by Prxs in this cestode, two genes for Prxs, identified in the genome of Taenia solium (TsPrx1 and TsPrx3), were cloned. The sequence of the proteins suggests that both isoforms belong to the class of typical Prxs 2-Cys. In addition, TsPrx3 harbors a mitochondrial localization signal peptide and two motifs (-GGLG- and -YP-) associated with overoxidation. Our kinetic characterization assigns them as thioredoxin peroxidases (TPxs). While TsPrx1 and TsPrx3 exhibit the same catalytic efficiency, thioredoxin–glutathione reductase from T. crassiceps (TcTGR) was five and eight times higher. Additionally, the latter demonstrated a lower affinity (>30-fold) for H2O2 in comparison with TsPrx1 and TsPrx3. The TcTGR contains a Sec residue in its C-terminal, which confers additional peroxidase activity. The aforementioned aspect implies that TsPrx1 and TsPrx3 are catalytically active at low H2O2 concentrations, and the TcTGR acts at high H2O2 concentrations. These results may explain why the T. crassiceps cysticerci can tolerate high H2O2 concentrations.

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Section: Kinetic Analysis Of Tctgrsupporting

confidence: 75%

A Physiological Approach to Explore How Thioredoxin–Glutathione Reductase (TGR) and Peroxiredoxin (Prx) Eliminate H2O2 in Cysticerci of Taenia

Guevara-Flores,

Nava-Balderas,

de Jesús Martínez-González

et al. 2024

Antioxidants

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“…An interesting observation on the Sec-dependent H-TrxR concerns to its ability to reduce Trx substrates from a diversity of sources, in addition to its cognate [ 144 , 149 ]. To explain this lack of specificity for its disulfide substrate, it has been proposed that the structural and electrostatic features of the Trx binding site were conserved through evolution [ 99 , 150 , 151 ]. In this sense, the environment surrounding α-helix 3 of eukaryotic Trx shows a high density of negatively charged residues, which is complementary to a positively charged α-helix at the binding site on H-TrxR [ 151 ].…”

Section: Disulfide Reductasesmentioning

confidence: 99%

“…In the larval stage of Echinococcus granulosus two isoforms of Trx has been reported [ 213 ], which are located at the cytosolic and the mitochondrial compartments. In the metacestode (cysticerci) stage of Taenia crassiceps , cytosolic Trx was purified and characterized [ 151 ]. The protein is similar in its properties to the mammalian homologue.…”

Section: Architecture Of Thiol-dependent Antioxidant Systems In Inmentioning

confidence: 99%

The Architecture of Thiol Antioxidant Systems among Invertebrate Parasites

et al. 2017

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The use of oxygen as the final electron acceptor in aerobic organisms results in an improvement in the energy metabolism. However, as a byproduct of the aerobic metabolism, reactive oxygen species are produced, leaving to the potential risk of an oxidative stress. To contend with such harmful compounds, living organisms have evolved antioxidant strategies. In this sense, the thiol-dependent antioxidant defense systems play a central role. In all cases, cysteine constitutes the major building block on which such systems are constructed, being present in redox substrates such as glutathione, thioredoxin, and trypanothione, as well as at the catalytic site of a variety of reductases and peroxidases. In some cases, the related selenocysteine was incorporated at selected proteins. In invertebrate parasites, antioxidant systems have evolved in a diversity of both substrates and enzymes, representing a potential area in the design of anti-parasite strategies. The present review focus on the organization of the thiol-based antioxidant systems in invertebrate parasites. Differences between these taxa and its final mammal host is stressed. An understanding of the antioxidant defense mechanisms in this kind of parasites, as well as their interactions with the specific host is crucial in the design of drugs targeting these organisms.

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

2019

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Purification and characterization of Taenia crassiceps cysticerci thioredoxin: insight into thioredoxin-glutathione-reductase (TGR) substrate recognition

Cited by 6 publications

References 80 publications

A Physiological Approach to Explore How Thioredoxin–Glutathione Reductase (TGR) and Peroxiredoxin (Prx) Eliminate H2O2 in Cysticerci of Taenia

A Physiological Approach to Explore How Thioredoxin–Glutathione Reductase (TGR) and Peroxiredoxin (Prx) Eliminate H2O2 in Cysticerci of Taenia

The Architecture of Thiol Antioxidant Systems among Invertebrate Parasites

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

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