Subcellular Proteomics and Global Analysis of Posttranslational Modifications to Study Functional Roles of Trypanosoma cruzi Molecules
Igor C. Almeida*, Ernesto S. Nakayasu*
Identifiers and Pagination:Year: 2010
First Page: 167
Last Page: 177
Publisher Id: TOPARAJ-4-167
Article History:Received Date: 15/11/2009
Revision Received Date: 1/5/2010
Acceptance Date: 3/5/2010
Electronic publication date: 10/12/2010
Collection year: 2010
open-access license: This is an open access article distributed under the terms of the Creative Commons Attribution 4.0 International Public License (CC-BY 4.0), a copy of which is available at: https://creativecommons.org/licenses/by/4.0/legalcode. This license permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
One century after the discovery of Chagas disease, the treatment for this illness is still based only on two drugs with limited efficacy and severe side effects. In this mini-review, we discuss the application of mass spectrometry (MS)- based proteomic approaches to study the biochemistry and cell biology of etiologic agent of Chagas disease, Trypanosoma cruzi. We focus the discussion in the analysis of subcellular proteomics and posttranslational modifications (PTMs). In recent years, subcellular proteomics has brought new insights into the localization of proteins and possible functions of organelles. Thus far, proteomic analysis of reservosomes, ribosomes, detergent-solubilized membranes, and a preparation of an organelle mixture have been performed. In addition, a number of analyses of PTMs of T. cruzi proteins (i.e., histone modifications, phosphorylation, glycosylation, glycosylphosphatidylinositol (GPI)-anchoring, and nitrosylation) have been successfully carried out. The identification of those and other PTMs combined with cutting-edge biochemical, immunological and cell biology approaches, have allowed a more in-depth understanding of biological and pathophysiological processes resulting from host cell-parasite interactions.