Functional analysis of cytosolic tryparedoxin peroxidase in antimony-resistant and –susceptible Leishmania braziliensis and Leishmania infantum lines

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Proteomic and Genomic Analyses of Antimony Resistant Leishmania infantum Mutant

BACKGROUND Antimonials remain the primary antileishmanial drugs in most developing countries. However, drug resistance to these compounds is increasing and our understanding of resistance mechanisms is partial. METHODS/PRINCIPAL FINDINGS In the present study, quantitative proteomics using stable isotope labelling of amino acids in cell culture (SILAC) and genome next generation sequencing wer...

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Mitochondrial Proteomics of Antimony and Miltefosine Resistant Leishmania infantum

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Tryparedoxin peroxidase of Leishmania braziliensis: homology modeling and inhibitory effects of flavonoids for anti-leishmanial activity

Inhibition of the Tryparedoxin peroxidase interaction has been becomes a new therapeutic strategy in leishmaniasis. Docking analysis was carried out to study the effects of quercetin and taxifolin on Tryparedoxin Peroxidase (TryP). Tryparedoxin peroxidase of Trypanosomatidae functions as antioxidants through their Peroxidase and peroxynitrite reductase activities. The 3D models of Tryparedoxin ...

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The role of dogs as reservoirs of Leishmania parasites, with emphasis on Leishmania (Leishmania) infantum and Leishmania (Viannia) braziliensis.

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Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of the mitochondrial tryparedoxin peroxidase from Leishmania braziliensis.

Tryparedoxin peroxidase (TXNPx) is an essential constituent of the main enzymatic scavenger system for reactive oxygen species (ROS) in trypanosomatids. Genetic studies have demonstrated the importance of this system for the development and virulence of these parasites, representing a potential target for the discovery of new trypanocidal drugs. In this work, the mitochondrial TXNPx from Leishm...

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ژورنال

عنوان ژورنال: Parasites & Vectors

سال: 2014

ISSN: 1756-3305

DOI: 10.1186/1756-3305-7-406