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BioMed Research International
Volume 2013 (2013), Article ID 493525, 11 pages
http://dx.doi.org/10.1155/2013/493525
Research Article

Identification of Protein Complex Associated with LYT1 of Trypanosoma cruzi

1Departamento de Biomedicina Molecular, Centro de Investigación y Estudios Avanzados del IPN, Avenida Instituto Politécnico Nacional No. 2508, Col. San Pedro Zacatenco, 07360 Gustavo A. Madero, DF, Mexico
2UBIMED, Facultad de Estudios Superiores Iztacala, Universidad Nacional Autónoma de México, Avenida De los Barrios 1, Col. Los Reyes Iztacala, 54090 Tlalnepantla, MEX, Mexico

Received 7 August 2012; Revised 21 December 2012; Accepted 24 December 2012

Academic Editor: Jorge Morales-Montor

Copyright © 2013 C. Lugo-Caballero et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Abstract

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.