Biochemical characterization of thioredoxin reductase from Babesia bovis

Regner, Erika Lucía; Thompson, Carolina S.; Iglesias, Alberto A.; Guerrero, Sandra; Arias, Diego Gustavo

doi:10.1016/j.biochi.2013.11.002

Cited by 9 publications

(3 citation statements)

References 40 publications

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“…According to Regner et al, the biochemical properties of proteins of the Trx system from the bovine parasite B. bovis , the Bbo Trx(R) system, share several features with their counterparts in P. falciparum , such as kinetics and physical properties and the capacity for reducing S -nitrosoglutathione (GSNO) and GSSG [ 26 ] ( Table 1 ).…”

Section: Babesia : Infection and Host Responsementioning

confidence: 99%

Oxidative Stress Control by Apicomplexan Parasites

Bosch

Kronenberger

Meissner

et al. 2015

BioMed Research International

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Section: Babesia : Infection and Host Responsementioning

confidence: 99%

Oxidative Stress Control by Apicomplexan Parasites

Bosch

Kronenberger

Meissner

et al. 2015

BioMed Research International

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“…To counteract Reactive Oxygen Species (ROS), Babesia employs anti-oxidant systems including Thioredoxinthioredoxin reductase (Trx/TrxR) and Glutathione-Glutathione Reductase (GSH/GR). Thioredoxin system comprises of Thioredoxin reductase (TrxR), various thioredoxins and Thioredoxin-dependent peroxidases (TPx).Thioredoxin reductase has been biochemically characterized in Babesia [7]. Thioredoxin reductase belongs to a family of dimeric flavoenzymes.…”

Section: Biomedical Research 2018; 29 (10): 2197-2214 Issn 0970-938x mentioning

confidence: 99%

Structural analysis of the Babesia microti thioredoxin reductase: a potential drug target for babesiosis treatment

Arora¹,

Banerjee²,

Narasu³

2018

biomedicalresearch

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Babesia microti, the causative agent of human babesiosis which was endemic in United States and parts of Europe with sporadic cases in other regions is expanding its geographical range. Being a common transfusion threat, Babesia has become a cause of concern in researchers and epidemiologists. Human babesiosis is now recognized as an emerging disease and gains more attention now than ever before. Thioredoxin reductase, a promising drug target in apicomplexan parasite has been validated in several species. This study focused on in-silico analysis of physicochemical properties, functional and structural aspects of thioredoxin reductase of B. microti. Comparative modeling approach was adopted for developing the three dimensional structural model of Thioredoxin reductase of Babesia microti. The model developed was found to be of reasonably good stereo-chemical quality by structure validation servers. This study will provide valuable insights about the function and structure of the enzyme thioredoxin reductase of B. microti and aid in developing effective chemotherapeutic agents for control and treatment of Babesia.

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“…Two distinct types of TrxRs have been described, both of them are dimeric proteins differing in their amino acid sequences and catalytic mechanisms. The first group includes low molecular mass TrxR (L-TrxR, 35 kDa per subunit), found in bacteria, plants and fungi [7]. L-TrxRs have a catalytic cycle that involves electrons transfer from NADPH to flavin and subsequently to the redox active disulfide, generating a dithiol [8,9].…”

Section: Introductionmentioning

confidence: 99%