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Elevated levels of tryparedoxin peroxidase in antimony unresponsive Leishmania donovani field isolates.

Susan Wyllie, Goutam Mandal, Neeloo Singh, Shyam Sundar, Alan H Fairlamb, Mitali Chatterjee

Division of Biological Chemistry and Drug Discovery, College of Life Sciences, University of Dundee, Dow Street, Dundee DD1 5EH Scotland, UK.

Journal Article: Molecular and Biochemical Parasitology (impact factor: 2.94). 10/2010; 173(2):162-4. DOI: 10.1016/j.molbiopara.2010.05.015

Abstract

Enhancement of the anti-oxidant metabolism of Leishmania parasites, dependent upon the unique dithiol trypanothione, has been implicated in laboratory-generated antimony resistance. Here, the role of the trypanothione-dependent anti-oxidant pathway is studied in antimony-resistant clinical isolates. Elevated levels of tryparedoxin and tryparedoxin peroxidase, key enzymes in hydroperoxide detoxification, were observed in antimonial resistant parasites resulting in an increased metabolism of peroxides. These data suggest that enhanced anti-oxidant defences may play a significant role in clinical resistance to antimonials.

Source: PubMed

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Keywords

antimonial resistant parasites
 
antimonials
 
antimony-resistant clinical
 
clinical resistance
 
key enzymes
 
laboratory-generated antimony resistance
 
Leishmania parasites
 
peroxides
 
trypanothione-dependent anti-oxidant pathway
 
tryparedoxin
 
tryparedoxin peroxidase
 
unique dithiol trypanothione