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

BMC Genomics

Research Article

Sophie Braga-Lagache¹  Manfred Heller¹  Torsten Ochsenreiter²  Daniel Wüthrich²  Kapila Gunasekera³ 

[1] Department of Clinical Research, University of Bern, Bern, Switzerland;Institute for Cell Biology, University of Bern, Bern, Switzerland;Institute for Cell Biology, University of Bern, Bern, Switzerland;Graduate School for Cellular and Biomedical Sciences, University of Bern, Bern, Switzerland;

关键词: Life Cycle Stage;    Bloodstream Form;    Dialyze Fetal Bovine Serum;    Stable Isotope Label Amino Acid;    Trypanosome Alternative Oxidase;   

DOI  :  10.1186/1471-2164-13-556

 received in 2012-07-27, accepted in 2012-10-11,  发布年份 2012

来源: Springer

【 摘 要 】

BackgroundTrypanosoma 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.ResultsUsing 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.ConclusionsWe 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.

【 授权许可】

Unknown   
© Gunasekera et al.; licensee BioMed Central Ltd. 2012. This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.