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pmid:28852088

Quantitative proteome and phosphoproteome analyses highlight the adherent population during Trypanosoma cruzi metacyclogenesis.

Juliana C Amorim · Michel Batista · Elizabeth S da Cunha · Aline C R Lucena · Carla V de Paula Lima · Karla Sousa · Marco A Krieger · Fabricio K Marchini

Scientific reports · 2017 doi:10.1038/s41598-017-10292-3

Paper

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Quantitative proteome and phosphoproteome analyses highlight the adherent population during Trypanosoma cruzi metacyclogenesis.
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10.1038/s41598-017-10292-3
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Juliana C Amorim
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Michel Batista
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Elizabeth S da Cunha
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Aline C R Lucena
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Carla V de Paula Lima
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Karla Sousa
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Marco A Krieger
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Fabricio K Marchini
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Scientific reports
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abstract
Trypanosoma cruzi metacyclogenesis is a natural process that occurs inside the triatomine vector and corresponds to the differentiation of non-infective epimastigotes into infective metacyclic trypomastigotes. The biochemical alterations necessary for the differentiation process have been widely studied with a focus on adhesion and nutritional stress. Here, using a mass spectrometry approach, a large-scale phospho(proteome) study was performed with the aim of understanding the metacyclogenesis processes in a quantitative manner. The results indicate that major modulations in the phospho(proteome) occur under nutritional stress and after 12 and 24 h of adhesion. Significant changes involve key cellular processes, such as translation, oxidative stress, and the metabolism of macromolecules, including proteins, lipids, and carbohydrates. Analysis of the signalling triggered by kinases and phosphatases from 7,336 identified phosphorylation sites demonstrates that 260 of these sites are modulated throughout the differentiation process, and some of these modulated proteins have previously been identified as drug targets in trypanosomiasis treatment. To the best of our knowledge, this study provides the first quantitative results highlighting the modulation of phosphorylation sites during metacyclogenesis and the greater coverage of the proteome to the parasite during this process. The data are available via ProteomeXchange with identifier number PXD006171.
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hesion and nutritional stress. Here, using a mass spectrometry approach, a large-scale phospho(proteome) st
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e protein and phosphosite quantitation using mass spectrometry was obtained through label free strategy pre
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frame, the time points selected for phospho(proteomic) analysis addressed various adherent time in
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clogenesis guide the experimental design The in vivo (Fig. 1A) and in vitro (Fig. 1B) metacycloge
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%, p < 0.05) and 72 to 96 h (5.8%), Fig. 1B. In vivo lifecycle highlighting the metacyclogenesis
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