Proteomic analysis of glycosomes from Trypanosoma cruzi epimastigotes

[Display omitted] •New metabolic routes and membrane proteins were identified in the organelles.•Exponential and stationary growth-phase cells vary little in glycosomal proteins.•A variety of proteins bearing a typical PTS1 but with unknown function were found. In Trypanosoma cruzi, the causal agent...

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Published in:Molecular and biochemical parasitology 2019-04, Vol.229, p.62-74
Main Authors: Acosta, Héctor, Burchmore, Richard, Naula, Christina, Gualdrón-López, Melisa, Quintero-Troconis, Ender, Cáceres, Ana J., Michels, Paul A.M., Concepción, Juan Luis, Quiñones, Wilfredo
Format: Article
Language:English
Subjects:
Cell fractionation
Chagas Disease - parasitology
Glycolysis
Glycosome
Life Cycle Stages
Mass spectrometry
Metabolism
Microbodies - chemistry
Microbodies - genetics
Microbodies - metabolism
Proteomics
Protozoan Proteins - chemistry
Protozoan Proteins - genetics
Protozoan Proteins - metabolism
Trypanosoma cruzi
Trypanosoma cruzi - chemistry
Trypanosoma cruzi - genetics
Trypanosoma cruzi - growth & development
Trypanosoma cruzi - metabolism
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Summary:[Display omitted] •New metabolic routes and membrane proteins were identified in the organelles.•Exponential and stationary growth-phase cells vary little in glycosomal proteins.•A variety of proteins bearing a typical PTS1 but with unknown function were found. 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 Na2CO3 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.
ISSN:0166-6851
1872-9428
DOI:10.1016/j.molbiopara.2019.02.008