Cargando…

Identification of Protein Complex Associated with LYT1 of Trypanosoma cruzi

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...

Descripción completa

Detalles Bibliográficos
Autores principales: Lugo-Caballero, C., Ballesteros-Rodea, G., Martínez-Calvillo, S., Manning-Cela, Rebeca
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Hindawi Publishing Corporation 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3613072/
https://www.ncbi.nlm.nih.gov/pubmed/23586042
http://dx.doi.org/10.1155/2013/493525
_version_ 1782264707836542976
author Lugo-Caballero, C.
Ballesteros-Rodea, G.
Martínez-Calvillo, S.
Manning-Cela, Rebeca
author_facet Lugo-Caballero, C.
Ballesteros-Rodea, G.
Martínez-Calvillo, S.
Manning-Cela, Rebeca
author_sort Lugo-Caballero, C.
collection PubMed
description 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.
format Online
Article
Text
id pubmed-3613072
institution National Center for Biotechnology Information
language English
publishDate 2013
publisher Hindawi Publishing Corporation
record_format MEDLINE/PubMed
spelling pubmed-36130722013-04-12 Identification of Protein Complex Associated with LYT1 of Trypanosoma cruzi Lugo-Caballero, C. Ballesteros-Rodea, G. Martínez-Calvillo, S. Manning-Cela, Rebeca Biomed Res Int Research Article 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. Hindawi Publishing Corporation 2013 2013-03-17 /pmc/articles/PMC3613072/ /pubmed/23586042 http://dx.doi.org/10.1155/2013/493525 Text en Copyright © 2013 C. Lugo-Caballero et al. https://creativecommons.org/licenses/by/3.0/ 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.
spellingShingle Research Article
Lugo-Caballero, C.
Ballesteros-Rodea, G.
Martínez-Calvillo, S.
Manning-Cela, Rebeca
Identification of Protein Complex Associated with LYT1 of Trypanosoma cruzi
title Identification of Protein Complex Associated with LYT1 of Trypanosoma cruzi
title_full Identification of Protein Complex Associated with LYT1 of Trypanosoma cruzi
title_fullStr Identification of Protein Complex Associated with LYT1 of Trypanosoma cruzi
title_full_unstemmed Identification of Protein Complex Associated with LYT1 of Trypanosoma cruzi
title_short Identification of Protein Complex Associated with LYT1 of Trypanosoma cruzi
title_sort identification of protein complex associated with lyt1 of trypanosoma cruzi
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3613072/
https://www.ncbi.nlm.nih.gov/pubmed/23586042
http://dx.doi.org/10.1155/2013/493525
work_keys_str_mv AT lugocaballeroc identificationofproteincomplexassociatedwithlyt1oftrypanosomacruzi
AT ballesterosrodeag identificationofproteincomplexassociatedwithlyt1oftrypanosomacruzi
AT martinezcalvillos identificationofproteincomplexassociatedwithlyt1oftrypanosomacruzi
AT manningcelarebeca identificationofproteincomplexassociatedwithlyt1oftrypanosomacruzi