Cargando…

Dynamic Association of ESCRT-II Proteins with ESCRT-I and ESCRT-III Complexes during Phagocytosis of Entamoeba histolytica

By their active movement and voraux phagocytosis, the trophozoites of Entamoeba histolytica constitute an excellent system to investigate the dynamics of the Endosomal Sorting Complex Required for Transport (ESCRT) protein interactions through phagocytosis. Here, we studied the proteins forming the...

Descripción completa

Detalles Bibliográficos
Autores principales: Díaz-Hernández, Mitzi, Javier-Reyna, Rosario, Martínez-Valencia, Diana, Montaño, Sarita, Orozco, Esther
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10049522/
https://www.ncbi.nlm.nih.gov/pubmed/36982336
http://dx.doi.org/10.3390/ijms24065267
_version_ 1785014478673281024
author Díaz-Hernández, Mitzi
Javier-Reyna, Rosario
Martínez-Valencia, Diana
Montaño, Sarita
Orozco, Esther
author_facet Díaz-Hernández, Mitzi
Javier-Reyna, Rosario
Martínez-Valencia, Diana
Montaño, Sarita
Orozco, Esther
author_sort Díaz-Hernández, Mitzi
collection PubMed
description By their active movement and voraux phagocytosis, the trophozoites of Entamoeba histolytica constitute an excellent system to investigate the dynamics of the Endosomal Sorting Complex Required for Transport (ESCRT) protein interactions through phagocytosis. Here, we studied the proteins forming the E. histolytica ESCRT-II complex and their relationship with other phagocytosis-involved molecules. Bioinformatics analysis predicted that EhVps22, EhVps25, and EhVps36 are E. histolytica bona fide orthologues of the ESCRT-II protein families. Recombinant proteins and specific antibodies revealed that ESCRT-II proteins interact with each other, with other ESCRT proteins, and phagocytosis-involved molecules, such as the adhesin (EhADH). Laser confocal microscopy, pull-down assays, and mass spectrometry analysis disclosed that during phagocytosis, ESCRT-II accompanies the red blood cells (RBCs) from their attachment to the trophozoites until their arrival to multivesicular bodies (MVBs), changing their interactive patterns according to the time and place of the process. Knocked-down trophozoites in the Ehvps25 gene presented a 50% lower rate of phagocytosis than the controls and lower efficiency to adhere RBCs. In conclusion, ESCRT-II interacts with other molecules during prey contact and conduction throughout the phagocytic channel and trophozoites membranous system. ESCRT-II proteins are members of the protein chain during vesicle trafficking and are fundamental for the continuity and efficiency of phagocytosis.
format Online
Article
Text
id pubmed-10049522
institution National Center for Biotechnology Information
language English
publishDate 2023
publisher MDPI
record_format MEDLINE/PubMed
spelling pubmed-100495222023-03-29 Dynamic Association of ESCRT-II Proteins with ESCRT-I and ESCRT-III Complexes during Phagocytosis of Entamoeba histolytica Díaz-Hernández, Mitzi Javier-Reyna, Rosario Martínez-Valencia, Diana Montaño, Sarita Orozco, Esther Int J Mol Sci Article By their active movement and voraux phagocytosis, the trophozoites of Entamoeba histolytica constitute an excellent system to investigate the dynamics of the Endosomal Sorting Complex Required for Transport (ESCRT) protein interactions through phagocytosis. Here, we studied the proteins forming the E. histolytica ESCRT-II complex and their relationship with other phagocytosis-involved molecules. Bioinformatics analysis predicted that EhVps22, EhVps25, and EhVps36 are E. histolytica bona fide orthologues of the ESCRT-II protein families. Recombinant proteins and specific antibodies revealed that ESCRT-II proteins interact with each other, with other ESCRT proteins, and phagocytosis-involved molecules, such as the adhesin (EhADH). Laser confocal microscopy, pull-down assays, and mass spectrometry analysis disclosed that during phagocytosis, ESCRT-II accompanies the red blood cells (RBCs) from their attachment to the trophozoites until their arrival to multivesicular bodies (MVBs), changing their interactive patterns according to the time and place of the process. Knocked-down trophozoites in the Ehvps25 gene presented a 50% lower rate of phagocytosis than the controls and lower efficiency to adhere RBCs. In conclusion, ESCRT-II interacts with other molecules during prey contact and conduction throughout the phagocytic channel and trophozoites membranous system. ESCRT-II proteins are members of the protein chain during vesicle trafficking and are fundamental for the continuity and efficiency of phagocytosis. MDPI 2023-03-09 /pmc/articles/PMC10049522/ /pubmed/36982336 http://dx.doi.org/10.3390/ijms24065267 Text en © 2023 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Díaz-Hernández, Mitzi
Javier-Reyna, Rosario
Martínez-Valencia, Diana
Montaño, Sarita
Orozco, Esther
Dynamic Association of ESCRT-II Proteins with ESCRT-I and ESCRT-III Complexes during Phagocytosis of Entamoeba histolytica
title Dynamic Association of ESCRT-II Proteins with ESCRT-I and ESCRT-III Complexes during Phagocytosis of Entamoeba histolytica
title_full Dynamic Association of ESCRT-II Proteins with ESCRT-I and ESCRT-III Complexes during Phagocytosis of Entamoeba histolytica
title_fullStr Dynamic Association of ESCRT-II Proteins with ESCRT-I and ESCRT-III Complexes during Phagocytosis of Entamoeba histolytica
title_full_unstemmed Dynamic Association of ESCRT-II Proteins with ESCRT-I and ESCRT-III Complexes during Phagocytosis of Entamoeba histolytica
title_short Dynamic Association of ESCRT-II Proteins with ESCRT-I and ESCRT-III Complexes during Phagocytosis of Entamoeba histolytica
title_sort dynamic association of escrt-ii proteins with escrt-i and escrt-iii complexes during phagocytosis of entamoeba histolytica
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10049522/
https://www.ncbi.nlm.nih.gov/pubmed/36982336
http://dx.doi.org/10.3390/ijms24065267
work_keys_str_mv AT diazhernandezmitzi dynamicassociationofescrtiiproteinswithescrtiandescrtiiicomplexesduringphagocytosisofentamoebahistolytica
AT javierreynarosario dynamicassociationofescrtiiproteinswithescrtiandescrtiiicomplexesduringphagocytosisofentamoebahistolytica
AT martinezvalenciadiana dynamicassociationofescrtiiproteinswithescrtiandescrtiiicomplexesduringphagocytosisofentamoebahistolytica
AT montanosarita dynamicassociationofescrtiiproteinswithescrtiandescrtiiicomplexesduringphagocytosisofentamoebahistolytica
AT orozcoesther dynamicassociationofescrtiiproteinswithescrtiandescrtiiicomplexesduringphagocytosisofentamoebahistolytica