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Open Access Highly Accessed Research article

Proteome remodelling during development from blood to insect-form Trypanosoma brucei quantified by SILAC and mass spectrometry

Kapila Gunasekera13, Daniel Wüthrich1, Sophie Braga-Lagache2, Manfred Heller2 and Torsten Ochsenreiter1*

Author affiliations

1 Institute for Cell Biology, University of Bern, Bern, Switzerland

2 Department of Clinical Research, University of Bern, Bern, Switzerland

3 Graduate School for Cellular and Biomedical Sciences, University of Bern, Bern, Switzerland

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Citation and License

BMC Genomics 2012, 13:556  doi:10.1186/1471-2164-13-556

Published: 16 October 2012

Abstract

Background

Trypanosoma brucei is the causative agent of human African sleeping sickness and Nagana in cattle. In addition to being an important pathogen T. brucei has developed into a model system in cell biology.

Results

Using Stable Isotope Labelling of Amino acids in Cell culture (SILAC) in combination with mass spectrometry we determined the abundance of >1600 proteins in the long slender (LS), short stumpy (SS) mammalian bloodstream form stages relative to the procyclic (PC) insect-form stage. In total we identified 2645 proteins, corresponding to ~30% of the total proteome and for the first time present a comprehensive overview of relative protein levels in three life stages of the parasite.

Conclusions

We can show the extent of pre-adaptation in the SS cells, especially at the level of the mitochondrial proteome. The comparison to a previously published report on monomorphic in vitro grown bloodstream and procyclic T. brucei indicates a loss of stringent regulation particularly of mitochondrial proteins in these cells when compared to the pleomorphic in vivo situation. In order to better understand the different levels of gene expression regulation in this organism we compared mRNA steady state abundance with the relative protein abundance-changes and detected moderate but significant correlation indicating that trypanosomes possess a significant repertoire of translational and posttranslational mechanisms to regulate protein abundance.