Proteomic analysis of glycosomes from Trypanosoma cruzi epimastigotes

Héctor Acosta, Richard Burchmore, Christina Naula, Melisa Gualdrón-López, Ender Quintero-Troconis, Ana J. Cáceres, Paul A.M. Michels, Juan Luis Concepción, Wilfredo Quiñones*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review


In Trypanosoma cruzi, the causal agent of Chagas disease, the first seven steps of glycolysis are compartmentalized in glycosomes, which are authentic but specialized peroxisomes. Besides glycolysis, activity of enzymes of other metabolic processes have been reported to be present in glycosomes, such as β-oxidation of fatty acids, purine salvage, pentose-phosphate pathway, gluconeogenesis and biosynthesis of ether-lipids, isoprenoids, sterols and pyrimidines. In this study, we have purified glycosomes from T. cruzi epimastigotes, collected the soluble and membrane fractions of these organelles, and separated peripheral and integral membrane proteins by Na 2 CO 3 treatment and osmotic shock. Proteomic analysis was performed on each of these fractions, allowing us to confirm the presence of enzymes involved in various metabolic pathways as well as identify new components of this parasite's glycosomes.

Original languageEnglish
Pages (from-to)62-74
Number of pages13
JournalMolecular and Biochemical Parasitology
Early online date1 Mar 2019
Publication statusPublished - Apr 2019


  • cell fractionation
  • glycolysis
  • glycosome
  • mass spectrometry
  • metabolism
  • proteomics
  • Trypanosoma cruzi


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