Cargando…
EhP3, a homolog of 14-3-3 family of protein participates in actin reorganization and phagocytosis in Entamoeba histolytica
The highly conserved proteins of the 14-3-3 family are universal adaptors known to regulate an enormous range of cellular processes in eukaryotes. However, their biological functions remain largely uncharacterized in pathogenic protists comprising of several 14-3-3 protein isoforms. In this study, w...
Autores principales: | , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2019
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6541287/ https://www.ncbi.nlm.nih.gov/pubmed/31095644 http://dx.doi.org/10.1371/journal.ppat.1007789 |
_version_ | 1783422748014411776 |
---|---|
author | Agarwal, Shalini Anand, Gaurav Sharma, Shalini Parimita Rath, Pragyan Gourinath, Samudrala Bhattacharya, Alok |
author_facet | Agarwal, Shalini Anand, Gaurav Sharma, Shalini Parimita Rath, Pragyan Gourinath, Samudrala Bhattacharya, Alok |
author_sort | Agarwal, Shalini |
collection | PubMed |
description | The highly conserved proteins of the 14-3-3 family are universal adaptors known to regulate an enormous range of cellular processes in eukaryotes. However, their biological functions remain largely uncharacterized in pathogenic protists comprising of several 14-3-3 protein isoforms. In this study, we report the role of 14-3-3 in coordinating cytoskeletal dynamics during phagocytosis in a professional phagocytic protist Entamoeba histolytica, the etiological agent of human amebiasis. There are three isoforms of 14-3-3 protein in amoeba and here we have investigated Eh14-3-3 Protein 3 (EhP3). Live and fixed cell imaging studies revealed the presence of this protein throughout the parasite phagocytosis process, with high rate of accumulation at the phagocytic cups and closed phagosomes. Conditional suppression of EhP3 expression caused significant defects in phagocytosis accompanied by extensive diminution of F-actin at the site of cup formation. Downregulated cells also exhibited defective recruitment of an F-actin stabilizing protein, EhCoactosin at the phagocytic cups. In addition, mass spectrometry based analysis further revealed a large group of EhP3-associated proteins, many of these proteins are known to regulate cytoskeletal architecture in E histolytica. The dynamics of these proteins may also be controlled by EhP3. Taken together, our findings strongly suggest that EhP3 is a novel and a key regulatory element of actin dynamics and phagocytosis in E. histolytica. |
format | Online Article Text |
id | pubmed-6541287 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-65412872019-06-05 EhP3, a homolog of 14-3-3 family of protein participates in actin reorganization and phagocytosis in Entamoeba histolytica Agarwal, Shalini Anand, Gaurav Sharma, Shalini Parimita Rath, Pragyan Gourinath, Samudrala Bhattacharya, Alok PLoS Pathog Research Article The highly conserved proteins of the 14-3-3 family are universal adaptors known to regulate an enormous range of cellular processes in eukaryotes. However, their biological functions remain largely uncharacterized in pathogenic protists comprising of several 14-3-3 protein isoforms. In this study, we report the role of 14-3-3 in coordinating cytoskeletal dynamics during phagocytosis in a professional phagocytic protist Entamoeba histolytica, the etiological agent of human amebiasis. There are three isoforms of 14-3-3 protein in amoeba and here we have investigated Eh14-3-3 Protein 3 (EhP3). Live and fixed cell imaging studies revealed the presence of this protein throughout the parasite phagocytosis process, with high rate of accumulation at the phagocytic cups and closed phagosomes. Conditional suppression of EhP3 expression caused significant defects in phagocytosis accompanied by extensive diminution of F-actin at the site of cup formation. Downregulated cells also exhibited defective recruitment of an F-actin stabilizing protein, EhCoactosin at the phagocytic cups. In addition, mass spectrometry based analysis further revealed a large group of EhP3-associated proteins, many of these proteins are known to regulate cytoskeletal architecture in E histolytica. The dynamics of these proteins may also be controlled by EhP3. Taken together, our findings strongly suggest that EhP3 is a novel and a key regulatory element of actin dynamics and phagocytosis in E. histolytica. Public Library of Science 2019-05-16 /pmc/articles/PMC6541287/ /pubmed/31095644 http://dx.doi.org/10.1371/journal.ppat.1007789 Text en © 2019 Agarwal 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 (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. |
spellingShingle | Research Article Agarwal, Shalini Anand, Gaurav Sharma, Shalini Parimita Rath, Pragyan Gourinath, Samudrala Bhattacharya, Alok EhP3, a homolog of 14-3-3 family of protein participates in actin reorganization and phagocytosis in Entamoeba histolytica |
title | EhP3, a homolog of 14-3-3 family of protein participates in actin reorganization and phagocytosis in Entamoeba histolytica |
title_full | EhP3, a homolog of 14-3-3 family of protein participates in actin reorganization and phagocytosis in Entamoeba histolytica |
title_fullStr | EhP3, a homolog of 14-3-3 family of protein participates in actin reorganization and phagocytosis in Entamoeba histolytica |
title_full_unstemmed | EhP3, a homolog of 14-3-3 family of protein participates in actin reorganization and phagocytosis in Entamoeba histolytica |
title_short | EhP3, a homolog of 14-3-3 family of protein participates in actin reorganization and phagocytosis in Entamoeba histolytica |
title_sort | ehp3, a homolog of 14-3-3 family of protein participates in actin reorganization and phagocytosis in entamoeba histolytica |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6541287/ https://www.ncbi.nlm.nih.gov/pubmed/31095644 http://dx.doi.org/10.1371/journal.ppat.1007789 |
work_keys_str_mv | AT agarwalshalini ehp3ahomologof1433familyofproteinparticipatesinactinreorganizationandphagocytosisinentamoebahistolytica AT anandgaurav ehp3ahomologof1433familyofproteinparticipatesinactinreorganizationandphagocytosisinentamoebahistolytica AT sharmashalini ehp3ahomologof1433familyofproteinparticipatesinactinreorganizationandphagocytosisinentamoebahistolytica AT parimitarathpragyan ehp3ahomologof1433familyofproteinparticipatesinactinreorganizationandphagocytosisinentamoebahistolytica AT gourinathsamudrala ehp3ahomologof1433familyofproteinparticipatesinactinreorganizationandphagocytosisinentamoebahistolytica AT bhattacharyaalok ehp3ahomologof1433familyofproteinparticipatesinactinreorganizationandphagocytosisinentamoebahistolytica |