A unique type of cyclic AMP-binding protein of Trypanosoma cruzi

Rangel-Aldao, Rafael; Allende, Oscar; Cayama, Edmundo

doi:10.1016/0166-6851(85)90107-0

Cited by 5 publications

(1 citation statement)

References 25 publications

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“…In order to unravel the mechanisms that mediate T. cruzi differentiation, it is essential to identify the molecules responsible for the intracellular signaling mechanisms that trigger the process in response to environmental changes (20). For instance, little is known about how cAMP molecules are involved in amastigogenesis; however, several studies have reported the involvement of this ubiquitous intracellular second messenger in the control of metacyclic trypomastigote differentiation in vitro (21).…”

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confidence: 99%

Quantitative Proteomic and Phosphoproteomic Analysis of Trypanosoma cruzi Amastigogenesis

Queiroz

Charneau

Mandacaru

et al. 2014

Molecular & Cellular Proteomics

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Chagas disease is a tropical neglected disease endemic in Latin America caused by the protozoan Trypanosoma cruzi. The parasite has four major life stages: epimastigote, metacyclic trypomastigote, bloodstream trypomastigote, and amastigote. The differentiation from infective trypomastigotes into replicative amastigotes, called amastigogenesis, takes place in vivo inside mammalian host cells after a period of incubation in an acidic phagolysosome. This differentiation process can be mimicked in vitro by incubating tissue-culture-derived trypomastigotes in acidic DMEM. Here we used this well-established differentiation protocol to perform a comprehensive quantitative proteomic and phosphoproteomic analysis of T. cruzi amastigogenesis. Samples from fully differentiated forms and two biologically relevant intermediate time points were Lys-C/trypsin digested, iTRAQ-labeled, and multiplexed. Subsequently, phosphopeptides were enriched using a TiO 2 matrix. Non-phosphorylated peptides were fractionated via hydrophilic interaction liquid chromatography prior to LC-MS/MS analysis. LC-MS/MS and bioinformatics procedures were used for protein and phosphopeptide quantitation, identification, and phosphorylation site assignment. We were able to identify regulated proteins and pathways involved in coordinating amastigogenesis. We also observed that a significant proportion of the regulated proteins were membrane proteins. Modulated phosphorylation events coordinated by protein kinases and phosphatases that are part of the signaling cascade induced by incubation in acidic medium were also evinced. To our knowledge, this work is the most comprehensive quantitative proteomics study of T. cruzi amastigogenesis, and these data will serve as a trustworthy basis for future studies, and possibly for new potential drug targets. Molecular & Cellular Proteomics 13:

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confidence: 99%