Cargando…

A Proteomic and Cellular Analysis of Uropods in the Pathogen Entamoeba histolytica

Exposure of Entamoeba histolytica to specific ligands induces cell polarization via the activation of signalling pathways and cytoskeletal elements. The process leads to formation of a protruding pseudopod at the front of the cell and a retracting uropod at the rear. In the present study, we show th...

Descripción completa

Detalles Bibliográficos
Autores principales: Marquay Markiewicz, Jacques, Syan, Sylvie, Hon, Chung-Chau, Weber, Christian, Faust, Daniela, Guillen, Nancy
Formato: Texto
Lenguaje:English
Publicado: Public Library of Science 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3071361/
https://www.ncbi.nlm.nih.gov/pubmed/21483708
http://dx.doi.org/10.1371/journal.pntd.0001002
_version_ 1782201442909552640
author Marquay Markiewicz, Jacques
Syan, Sylvie
Hon, Chung-Chau
Weber, Christian
Faust, Daniela
Guillen, Nancy
author_facet Marquay Markiewicz, Jacques
Syan, Sylvie
Hon, Chung-Chau
Weber, Christian
Faust, Daniela
Guillen, Nancy
author_sort Marquay Markiewicz, Jacques
collection PubMed
description Exposure of Entamoeba histolytica to specific ligands induces cell polarization via the activation of signalling pathways and cytoskeletal elements. The process leads to formation of a protruding pseudopod at the front of the cell and a retracting uropod at the rear. In the present study, we show that the uropod forms during the exposure of trophozoites to serum isolated from humans suffering of amoebiasis. To investigate uropod assembly, we used LC-MS/MS technology to identify protein components in isolated uropod fractions. The galactose/N-acetylgalactosamine lectin, the immunodominant antigen M17 (which is specifically recognized by serum from amoeba-infected persons) and a few other cells adhesion-related molecules were primarily involved. Actin-rich cytoskeleton components, GTPases from the Rac and Rab families, filamin, α-actinin and a newly identified ezrin-moesin-radixin protein were the main factors found to potentially interact with capped receptors. A set of specific cysteine proteases and a serine protease were enriched in isolated uropod fractions. However, biological assays indicated that cysteine proteases are not involved in uropod formation in E. histolytica, a fact in contrast to the situation in human motile immune cells. The surface proteins identified here are testable biomarkers which may be either recognized by the immune system and/or released into the circulation during amoebiasis.
format Text
id pubmed-3071361
institution National Center for Biotechnology Information
language English
publishDate 2011
publisher Public Library of Science
record_format MEDLINE/PubMed
spelling pubmed-30713612011-04-11 A Proteomic and Cellular Analysis of Uropods in the Pathogen Entamoeba histolytica Marquay Markiewicz, Jacques Syan, Sylvie Hon, Chung-Chau Weber, Christian Faust, Daniela Guillen, Nancy PLoS Negl Trop Dis Research Article Exposure of Entamoeba histolytica to specific ligands induces cell polarization via the activation of signalling pathways and cytoskeletal elements. The process leads to formation of a protruding pseudopod at the front of the cell and a retracting uropod at the rear. In the present study, we show that the uropod forms during the exposure of trophozoites to serum isolated from humans suffering of amoebiasis. To investigate uropod assembly, we used LC-MS/MS technology to identify protein components in isolated uropod fractions. The galactose/N-acetylgalactosamine lectin, the immunodominant antigen M17 (which is specifically recognized by serum from amoeba-infected persons) and a few other cells adhesion-related molecules were primarily involved. Actin-rich cytoskeleton components, GTPases from the Rac and Rab families, filamin, α-actinin and a newly identified ezrin-moesin-radixin protein were the main factors found to potentially interact with capped receptors. A set of specific cysteine proteases and a serine protease were enriched in isolated uropod fractions. However, biological assays indicated that cysteine proteases are not involved in uropod formation in E. histolytica, a fact in contrast to the situation in human motile immune cells. The surface proteins identified here are testable biomarkers which may be either recognized by the immune system and/or released into the circulation during amoebiasis. Public Library of Science 2011-04-05 /pmc/articles/PMC3071361/ /pubmed/21483708 http://dx.doi.org/10.1371/journal.pntd.0001002 Text en Marquay Markiewicz et al. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Marquay Markiewicz, Jacques
Syan, Sylvie
Hon, Chung-Chau
Weber, Christian
Faust, Daniela
Guillen, Nancy
A Proteomic and Cellular Analysis of Uropods in the Pathogen Entamoeba histolytica
title A Proteomic and Cellular Analysis of Uropods in the Pathogen Entamoeba histolytica
title_full A Proteomic and Cellular Analysis of Uropods in the Pathogen Entamoeba histolytica
title_fullStr A Proteomic and Cellular Analysis of Uropods in the Pathogen Entamoeba histolytica
title_full_unstemmed A Proteomic and Cellular Analysis of Uropods in the Pathogen Entamoeba histolytica
title_short A Proteomic and Cellular Analysis of Uropods in the Pathogen Entamoeba histolytica
title_sort proteomic and cellular analysis of uropods in the pathogen entamoeba histolytica
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3071361/
https://www.ncbi.nlm.nih.gov/pubmed/21483708
http://dx.doi.org/10.1371/journal.pntd.0001002
work_keys_str_mv AT marquaymarkiewiczjacques aproteomicandcellularanalysisofuropodsinthepathogenentamoebahistolytica
AT syansylvie aproteomicandcellularanalysisofuropodsinthepathogenentamoebahistolytica
AT honchungchau aproteomicandcellularanalysisofuropodsinthepathogenentamoebahistolytica
AT weberchristian aproteomicandcellularanalysisofuropodsinthepathogenentamoebahistolytica
AT faustdaniela aproteomicandcellularanalysisofuropodsinthepathogenentamoebahistolytica
AT guillennancy aproteomicandcellularanalysisofuropodsinthepathogenentamoebahistolytica
AT marquaymarkiewiczjacques proteomicandcellularanalysisofuropodsinthepathogenentamoebahistolytica
AT syansylvie proteomicandcellularanalysisofuropodsinthepathogenentamoebahistolytica
AT honchungchau proteomicandcellularanalysisofuropodsinthepathogenentamoebahistolytica
AT weberchristian proteomicandcellularanalysisofuropodsinthepathogenentamoebahistolytica
AT faustdaniela proteomicandcellularanalysisofuropodsinthepathogenentamoebahistolytica
AT guillennancy proteomicandcellularanalysisofuropodsinthepathogenentamoebahistolytica