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EhCoactosin Stabilizes Actin Filaments in the Protist Parasite Entamoeba histolytica

Entamoeba histolytica is a protist parasite that is the causative agent of amoebiasis, and is a highly motile organism. The motility is essential for its survival and pathogenesis, and a dynamic actin cytoskeleton is required for this process. EhCoactosin, an actin-binding protein of the ADF/cofilin...

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Autores principales: Kumar, Nitesh, Somlata, Mazumder, Mohit, Dutta, Priyanka, Maiti, Sankar, Gourinath, Samudrala
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4161475/
https://www.ncbi.nlm.nih.gov/pubmed/25210743
http://dx.doi.org/10.1371/journal.ppat.1004362
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author Kumar, Nitesh
Somlata,
Mazumder, Mohit
Dutta, Priyanka
Maiti, Sankar
Gourinath, Samudrala
author_facet Kumar, Nitesh
Somlata,
Mazumder, Mohit
Dutta, Priyanka
Maiti, Sankar
Gourinath, Samudrala
author_sort Kumar, Nitesh
collection PubMed
description Entamoeba histolytica is a protist parasite that is the causative agent of amoebiasis, and is a highly motile organism. The motility is essential for its survival and pathogenesis, and a dynamic actin cytoskeleton is required for this process. EhCoactosin, an actin-binding protein of the ADF/cofilin family, participates in actin dynamics, and here we report our studies of this protein using both structural and functional approaches. The X-ray crystal structure of EhCoactosin resembles that of human coactosin-like protein, with major differences in the distribution of surface charges and the orientation of terminal regions. According to in vitro binding assays, full-length EhCoactosin binds both F- and G-actin. Instead of acting to depolymerize or severe F-actin, EhCoactosin directly stabilizes the polymer. When EhCoactosin was visualized in E. histolytica cells using either confocal imaging or total internal reflectance microscopy, it was found to colocalize with F-actin at phagocytic cups. Over-expression of this protein stabilized F-actin and inhibited the phagocytic process. EhCoactosin appears to be an unusual type of coactosin involved in E. histolytica actin dynamics.
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spelling pubmed-41614752014-09-17 EhCoactosin Stabilizes Actin Filaments in the Protist Parasite Entamoeba histolytica Kumar, Nitesh Somlata, Mazumder, Mohit Dutta, Priyanka Maiti, Sankar Gourinath, Samudrala PLoS Pathog Research Article Entamoeba histolytica is a protist parasite that is the causative agent of amoebiasis, and is a highly motile organism. The motility is essential for its survival and pathogenesis, and a dynamic actin cytoskeleton is required for this process. EhCoactosin, an actin-binding protein of the ADF/cofilin family, participates in actin dynamics, and here we report our studies of this protein using both structural and functional approaches. The X-ray crystal structure of EhCoactosin resembles that of human coactosin-like protein, with major differences in the distribution of surface charges and the orientation of terminal regions. According to in vitro binding assays, full-length EhCoactosin binds both F- and G-actin. Instead of acting to depolymerize or severe F-actin, EhCoactosin directly stabilizes the polymer. When EhCoactosin was visualized in E. histolytica cells using either confocal imaging or total internal reflectance microscopy, it was found to colocalize with F-actin at phagocytic cups. Over-expression of this protein stabilized F-actin and inhibited the phagocytic process. EhCoactosin appears to be an unusual type of coactosin involved in E. histolytica actin dynamics. Public Library of Science 2014-09-11 /pmc/articles/PMC4161475/ /pubmed/25210743 http://dx.doi.org/10.1371/journal.ppat.1004362 Text en © 2014 Kumar 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
Kumar, Nitesh
Somlata,
Mazumder, Mohit
Dutta, Priyanka
Maiti, Sankar
Gourinath, Samudrala
EhCoactosin Stabilizes Actin Filaments in the Protist Parasite Entamoeba histolytica
title EhCoactosin Stabilizes Actin Filaments in the Protist Parasite Entamoeba histolytica
title_full EhCoactosin Stabilizes Actin Filaments in the Protist Parasite Entamoeba histolytica
title_fullStr EhCoactosin Stabilizes Actin Filaments in the Protist Parasite Entamoeba histolytica
title_full_unstemmed EhCoactosin Stabilizes Actin Filaments in the Protist Parasite Entamoeba histolytica
title_short EhCoactosin Stabilizes Actin Filaments in the Protist Parasite Entamoeba histolytica
title_sort ehcoactosin stabilizes actin filaments in the protist parasite entamoeba histolytica
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4161475/
https://www.ncbi.nlm.nih.gov/pubmed/25210743
http://dx.doi.org/10.1371/journal.ppat.1004362
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