2015
DOI: 10.1590/0074-02760150024
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Trypanosoma evansi is alike to Trypanosoma brucei brucei in the subcellular localisation of glycolytic enzymes

Abstract: Trypanosoma evansi, which causes surra, is descended from Trypanosoma brucei brucei, which causes nagana. Although both parasites are presumed to be metabolically similar, insufficient knowledge of T. evansi precludes a full comparison. Herein, we provide the first report on the subcellular localisation of the glycolytic enzymes in T. evansi, which is a alike to that of the bloodstream form (BSF) of T. b. brucei: (i) fructose-bisphosphate aldolase, glyceraldehyde-3-phosphate dehydrogenase (GAPDH), hexokinase, … Show more

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Cited by 9 publications
(2 citation statements)
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“…Trypanosoma evansi is thought to have evolved from T. brucei by completely losing kinetoplast maxicircles which are involved in morphological development and multiplication within tsetse flies. These trypanosomes are thus independent of tsetse transmission (Moreno and Nava, 2015).…”
Section: Introductionmentioning
confidence: 96%
“…Trypanosoma evansi is thought to have evolved from T. brucei by completely losing kinetoplast maxicircles which are involved in morphological development and multiplication within tsetse flies. These trypanosomes are thus independent of tsetse transmission (Moreno and Nava, 2015).…”
Section: Introductionmentioning
confidence: 96%
“…The enzymes catalyzing the last three glycolytic reactions (phosphoglycerate mutase, enolase, and pyruvate kinase) have a cytosolic location and are not part of the glycosomal machinery. This is the case for both T. b. brucei and T. evansi , two evolutionary related Trypanozoon parasites [ 48 ] displaying an identical subcellular localization of their glycolytic enzymes [ 49 , 50 ]. ENO is a glycolytic enzyme that catalyzes the reversible conversion of D -2-phosphoglycerate to phosphoenolpyruvate.…”
Section: Introductionmentioning
confidence: 99%