Abstract HTML Views: 439 PDF Downloads: 137 Total Views/Downloads: 778
Abstract HTML Views: 309 PDF Downloads: 100 Total Views/Downloads: 573
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.