Profiling the Trypanosoma cruzi Phosphoproteome
Author Information
Author(s): Marchini Fabricio K., de Godoy Lyris M. F., Rampazzo Rita C. P., Pavoni Daniela P., Probst Christian M., Gnad Florian, Mann Matthias, Krieger Marco A.
Primary Institution: Instituto Carlos Chagas, Fiocruz, Curitiba, Paraná, Brazil
Hypothesis
To characterize the phosphoproteome of Trypanosoma cruzi during its differentiation process.
Conclusion
The study identified 1,671 proteins, including 753 phosphoproteins with 2,572 phosphorylation sites, providing the most comprehensive dataset for Kinetoplastida species to date.
Supporting Evidence
- 1,671 proteins were identified, including 753 phosphoproteins.
- A total of 2,572 phosphorylation sites were reported.
- The phosphoproteome dataset is the most comprehensive for Kinetoplastida species.
- Phosphorylation sites were predominantly found on serine residues.
Takeaway
Researchers studied a tiny bug that causes Chagas disease to see how its proteins change when it becomes infectious, finding lots of important changes.
Methodology
Mass spectrometry was used to analyze protein samples from T. cruzi at different differentiation stages, with phosphopeptides enriched using TiO2 chromatography.
Limitations
The study's data is not quantitative and relies on time points rather than continuous measurement.
Statistical Information
P-Value
p<0.05
Statistical Significance
p<0.05
Digital Object Identifier (DOI)
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