Trypanosoma evansi contains two auxiliary enzymes of glycolytic metabolism: Phosphoenolpyruvate carboxykinase and pyruvate phosphate dikinase.
Abstract: Trypanosoma evansi is a monomorphic protist that can infect horses and other animal species of economic importance for man. Like the bloodstream form of the closely related species Trypanosoma brucei, T. evansi depends exclusively on glycolysis for its free-energy generation. In T. evansi as in other kinetoplastid organisms, the enzymes of the major part of the glycolytic pathway are present within organelles called glycosomes, which are authentic but specialized peroxisomes. Since T. evansi does not undergo stage-dependent differentiations, it occurs only as bloodstream forms, it has been assumed that the metabolic pattern of this parasite is identical to that of the bloodstream form of T. brucei. However, we report here the presence of two additional enzymes, phosphoenolpyruvate carboxykinase and PPi-dependent pyruvate phosphate dikinase in T. evansi glycosomes. Their colocalization with glycolytic enzymes within the glycosomes of this parasite has not been reported before. Both enzymes can make use of PEP for contributing to the production of ATP within the organelles. The activity of these enzymes in T. evansi glycosomes drastically changes the model assumed for the oxidation of glucose by this parasite.
Copyright © 2016 Elsevier Inc. All rights reserved.
Publication Date: 2016-03-09 PubMed ID: 26968775DOI: 10.1016/j.exppara.2016.03.003Google Scholar: Lookup
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Summary
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The study reveals that Trypanosoma evansi, a protozoan that infects various animal species, has two additional enzymes in its glycolytic metabolic processes than previously identified. These findings significantly alter the understanding of glucose oxidation in this parasite.
Background
- Trypanosoma evansi is a single-celled parasite that infects various animals, including horses, which has economic implications.
- Being monomorphic, T. evansi does not exhibit stage-by-stage differentiation. Because of its similarity to the Trypanosoma brucei species, it was assumed to exhibit the same metabolic processes.
- Largely dependent on glycolysis for energy generation, T. evansi carries out this process within organelles known as glycosomes – specialized peroxisomes found in this and similar organisms.
New Findings
- The researchers discovered the presence of two additional enzymes, phosphoenolpyruvate carboxykinase, and PPi-dependent pyruvate phosphate dikinase, within the glycosomes of T. evansi.
- This is the first report of these enzymes in association with the glycolytic process within T. evansi’s glycosomes.
- Both enzymes utilize phosphoenolpyruvate (PEP) to potentially contribute to ATP production within the organelles, thus playing a critical role in the parasite’s energy generation.
Impact and Significance
- The unexpected presence of these enzymes notably changes the model for the oxidation of glucose in T. evansi.
- This discovery provides a new insight into the metabolic functions of T. evansi – specifically, its energy production methods.
- Understanding the metabolic processes in T. evansi, and similar parasites, can contribute to developing more effective treatment measures.
Cite This Article
APA
Rivero LA, Concepción JL, Quintero-Troconis E, Quiñones W, Michels PA, Acosta H.
(2016).
Trypanosoma evansi contains two auxiliary enzymes of glycolytic metabolism: Phosphoenolpyruvate carboxykinase and pyruvate phosphate dikinase.
Exp Parasitol, 165, 7-15.
https://doi.org/10.1016/j.exppara.2016.03.003 Publication
Researcher Affiliations
- Laboratorio de Enzimología de Parásitos, Facultad de Ciencias, Universidad de Los Andes, Mérida 5101, Venezuela.
- Laboratorio de Enzimología de Parásitos, Facultad de Ciencias, Universidad de Los Andes, Mérida 5101, Venezuela.
- Laboratorio de Enzimología de Parásitos, Facultad de Ciencias, Universidad de Los Andes, Mérida 5101, Venezuela.
- Laboratorio de Enzimología de Parásitos, Facultad de Ciencias, Universidad de Los Andes, Mérida 5101, Venezuela.
- Centre for Immunity, Infection and Evolution, and Centre for Translational and Chemical Biology, School of Biological Sciences, University of Edinburgh, United Kingdom.
- Laboratorio de Enzimología de Parásitos, Facultad de Ciencias, Universidad de Los Andes, Mérida 5101, Venezuela. Electronic address: hectoracosta@ula.ve.
MeSH Terms
- Animals
- Digitonin / pharmacology
- Glucosephosphate Dehydrogenase / isolation & purification
- Glucosephosphate Dehydrogenase / metabolism
- Glycolysis
- Hexokinase / isolation & purification
- Hexokinase / metabolism
- Horses
- Indicators and Reagents / pharmacology
- Malate Dehydrogenase / isolation & purification
- Malate Dehydrogenase / metabolism
- Mice
- Microbodies / enzymology
- Microscopy, Fluorescence
- Permeability / drug effects
- Phosphoenolpyruvate Carboxykinase (ATP) / genetics
- Phosphoenolpyruvate Carboxykinase (ATP) / isolation & purification
- Phosphoenolpyruvate Carboxykinase (ATP) / metabolism
- Phosphoglycerate Kinase / isolation & purification
- Phosphoglycerate Kinase / metabolism
- Phosphopyruvate Hydratase / isolation & purification
- Phosphopyruvate Hydratase / metabolism
- Pyruvate, Orthophosphate Dikinase / isolation & purification
- Pyruvate, Orthophosphate Dikinase / metabolism
- Rabbits
- Rats
- Rats, Wistar
- Trypanosoma / drug effects
- Trypanosoma / enzymology
Citations
This article has been cited 4 times.- Magez S, Li Z, Nguyen HTT, Pinto Torres JE, Van Wielendaele P, Radwanska M, Began J, Zoll S, Sterckx YG. The History of Anti-Trypanosome Vaccine Development Shows That Highly Immunogenic and Exposed Pathogen-Derived Antigens Are Not Necessarily Good Target Candidates: Enolase and ISG75 as Examples.. Pathogens 2021 Aug 19;10(8).
- Koendjbiharie JG, van Kranenburg R, Kengen SWM. The PEP-pyruvate-oxaloacetate node: variation at the heart of metabolism.. FEMS Microbiol Rev 2021 May 5;45(3).
- Rojas-Pirela M, Andrade-Alviárez D, Rojas V, Kemmerling U, Cáceres AJ, Michels PA, Concepción JL, Quiñones W. Phosphoglycerate kinase: structural aspects and functions, with special emphasis on the enzyme from Kinetoplastea.. Open Biol 2020 Nov;10(11):200302.
- Kovářová J, Nagar R, Faria J, Ferguson MAJ, Barrett MP, Horn D. Gluconeogenesis using glycerol as a substrate in bloodstream-form Trypanosoma brucei.. PLoS Pathog 2018 Dec;14(12):e1007475.
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