» Articles » PMID: 18696100

All Trypanosoma Cruzi Developmental Forms Present Lysosome-related Organelles

Overview
Publisher Springer
Date 2008 Aug 13
PMID 18696100
Citations 25
Authors
Affiliations
Soon will be listed here.
Abstract

Trypanosoma cruzi epimastigote forms concentrate their major protease, cruzipain, in the same compartment where these parasites store macromolecules obtained from medium and for this ability these organelles were named as reservosomes. Intracellular digestion occurs mainly inside reservosomes and seems to be modulated by cruzipain and its natural inhibitor chagasin that also concentrates in reservosomes. T. cruzi mammalian forms, trypomastigotes and amastigotes, are unable to capture macromolecules by endocytosis, but also express cruzipain and chagasin, whose role in infectivity has been described. In this paper, we demonstrate that trypomastigotes and amastigotes also concentrate cruzipain, chagasin as well as serine carboxypeptidase in hydrolase-rich compartments of acidic nature. The presence of P-type proton ATPase indicates that this compartment is acidified by the same enzyme as epimastigote endocytic compartments. Electron microscopy analyzes showed that these organelles are placed at the posterior region of the parasite body, are single membrane bound and possess an electron-dense matrix with electronlucent inclusions. Three-dimensional reconstruction showed that these compartments have different size and shape in trypomastigotes and amastigotes. Based on these evidences, we suggest that all T. cruzi developmental stages present lysosome-related organelles that in epimastigotes have the additional and unique ability of storing cargo.

Citing Articles

A versatile 2A peptide-based strategy for ectopic expression and endogenous gene tagging in .

Niemirowicz G, Carlevaro G, Campetella O, Bouvier L, Mucci J Heliyon. 2024; 10(2):e24595.

PMID: 38304823 PMC: 10830525. DOI: 10.1016/j.heliyon.2024.e24595.


Transcriptomic analysis of the adaptation to prolonged starvation of the insect-dwelling epimastigotes.

Smircich P, Perez-Diaz L, Hernandez F, Duhagon M, Garat B Front Cell Infect Microbiol. 2023; 13:1138456.

PMID: 37091675 PMC: 10117895. DOI: 10.3389/fcimb.2023.1138456.


Lysosome assembly and disassembly changes endocytosis rate through the Leishmania cell cycle.

Wang Z, Wheeler R, Sunter J Microbiologyopen. 2019; 9(2):e969.

PMID: 31743959 PMC: 7002101. DOI: 10.1002/mbo3.969.


Detection of Weakly Expressed Trypanosoma cruzi Membrane Proteins Using High-Performance Probes.

Cruz-Bustos T, Moreno S, Docampo R J Eukaryot Microbiol. 2018; 65(5):722-728.

PMID: 29542839 PMC: 6120783. DOI: 10.1111/jeu.12517.


Trypanosoma cruzi serinecarboxipeptidase is a sulfated glycoprotein and a minor antigen in human Chagas disease infection.

Soprano L, Parente J, Landoni M, Couto A, Duschak V Med Microbiol Immunol. 2017; 207(2):117-128.

PMID: 29274017 DOI: 10.1007/s00430-017-0529-7.


References
1.
Engel J, Torres C, Hsieh I, Doyle P, McKerrow J, Garcia C . Upregulation of the secretory pathway in cysteine protease inhibitor-resistant Trypanosoma cruzi. J Cell Sci. 2000; 113 ( Pt 8):1345-54. DOI: 10.1242/jcs.113.8.1345. View

2.
Adade C, de Castro S, Soares M . Ultrastructural localization of Trypanosoma cruzi lysosomes by aryl sulphatase cytochemistry. Micron. 2006; 38(3):252-6. DOI: 10.1016/j.micron.2006.05.002. View

3.
Engel J, Doyle P, Palmer J, Hsieh I, BAINTON D, McKerrow J . Cysteine protease inhibitors alter Golgi complex ultrastructure and function in Trypanosoma cruzi. J Cell Sci. 1998; 111 ( Pt 5):597-606. DOI: 10.1242/jcs.111.5.597. View

4.
De Souza W . Basic cell biology of Trypanosoma cruzi. Curr Pharm Des. 2002; 8(4):269-85. DOI: 10.2174/1381612023396276. View

5.
Raposo G, Marks M, Cutler D . Lysosome-related organelles: driving post-Golgi compartments into specialisation. Curr Opin Cell Biol. 2007; 19(4):394-401. PMC: 2782641. DOI: 10.1016/j.ceb.2007.05.001. View