Identification of protein complex associated with LYT1 of Trypanosoma cruzi
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To carry out the intracellular phase of its life cycle, Trypanosoma cruzi must infect a host cell. Although a few molecules have been reported to participate in this process, one known protein is LYT1, which promotes lysis under acidic conditions and is involved in parasite infection and development. Alternative transcripts from a single LYT1 gene generate two proteins with differential functions and compartmentalization. Single-gene products targeted to more than one location can interact with disparate proteins that might affect their function and targeting properties. The aim of this work was to study the LYT1 interaction map using coimmunoprecipitation assays with transgenic parasites expressing LYT1 products fused to GFP. We detected several proteins of sizes from 8 to 150 kDa that bind to LYT1 with different binding strengths. By MS-MS analysis, we identified proteins involved in parasite infectivity (trans-sialidase), development (kDSPs and histones H2A and H2B), and motility and protein traffic (dynein and α- and β-tubulin), as well as protein-protein interactions (TPR-protein and kDSPs) and several hypothetical proteins. Our approach led us to identify the LYT1 interaction profile, thereby providing insights into the molecular mechanisms that contribute to parasite stage development and pathogenesis of T. cruzi infection. © 2013 C. Lugo-Caballero et al.
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alpha tubulin; bacterial protein; beta tubulin; histone; protein LYT1; sialidase; unclassified drug; LYT1 protein, Trypanosoma cruzi; protozoal protein; article; gene product; immunoprecipitation; molecular mechanics; nonhuman; parasitosis; protein analysis; protein interaction; transgenic organism; Trypanosoma cruzi; Chagas disease; cytoplasm; genetics; host parasite interaction; human; metabolism; parasitology; pathogenicity; protein binding; protein protein interaction; tandem mass spectrometry; Trypanosoma cruzi; Chagas Disease; Cytoplasm; Host-Parasite Interactions; Humans; Protein Binding; Protein Interaction Maps; Protozoan Proteins; Tandem Mass Spectrometry; Trypanosoma cruzi
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