Cargando…

Identification of new components of the basal pole of Toxoplasma gondii provides novel insights into its molecular organization and functions

The Toxoplasma gondii tachyzoite is a singled-cell obligate intracellular parasite responsible for the acute phase of toxoplasmosis. This polarized cell exhibits an apical complex, a hallmark of the phylum Apicomplexa, essential for motility, invasion, and egress from the host cell. Located on the o...

Descripción completa

Detalles Bibliográficos
Autores principales: Roumégous, Chloé, Abou Hammoud, Aya, Fuster, Damien, Dupuy, Jean-William, Blancard, Corinne, Salin, Bénédicte, Robinson, Derrick R., Renesto, Patricia, Tardieux, Isabelle, Frénal, Karine
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9613666/
https://www.ncbi.nlm.nih.gov/pubmed/36310866
http://dx.doi.org/10.3389/fcimb.2022.1010038
_version_ 1784820025402589184
author Roumégous, Chloé
Abou Hammoud, Aya
Fuster, Damien
Dupuy, Jean-William
Blancard, Corinne
Salin, Bénédicte
Robinson, Derrick R.
Renesto, Patricia
Tardieux, Isabelle
Frénal, Karine
author_facet Roumégous, Chloé
Abou Hammoud, Aya
Fuster, Damien
Dupuy, Jean-William
Blancard, Corinne
Salin, Bénédicte
Robinson, Derrick R.
Renesto, Patricia
Tardieux, Isabelle
Frénal, Karine
author_sort Roumégous, Chloé
collection PubMed
description The Toxoplasma gondii tachyzoite is a singled-cell obligate intracellular parasite responsible for the acute phase of toxoplasmosis. This polarized cell exhibits an apical complex, a hallmark of the phylum Apicomplexa, essential for motility, invasion, and egress from the host cell. Located on the opposite end of the cell is the basal complex, an elaborated cytoskeletal structure that also plays critical roles in the lytic cycle of the parasite, being involved in motility, cell division, constriction and cytokinesis, as well as intravacuolar cell-cell communication. Nevertheless, only a few proteins of this structure have been described and functionally assessed. In this study, we used spatial proteomics to identify new basal complex components (BCC), and in situ imaging, including ultrastructure expansion microscopy, to position them. We thus confirmed the localization of nine BCCs out of the 12 selected candidates and assigned them to different sub-compartments of the basal complex, including two new domains located above the basal ring and below the posterior cup. Their functional investigation revealed that none of these BCCs are essential for parasite growth in vitro. However, one BCC is critical for constricting of the basal complex, likely through direct interaction with the class VI myosin heavy chain J (MyoJ), and for gliding motility. Four other BCCs, including a phosphatase and a guanylate-binding protein, are involved in the formation and/or maintenance of the intravacuolar parasite connection, which is required for the rosette organization and synchronicity of cell division.
format Online
Article
Text
id pubmed-9613666
institution National Center for Biotechnology Information
language English
publishDate 2022
publisher Frontiers Media S.A.
record_format MEDLINE/PubMed
spelling pubmed-96136662022-10-29 Identification of new components of the basal pole of Toxoplasma gondii provides novel insights into its molecular organization and functions Roumégous, Chloé Abou Hammoud, Aya Fuster, Damien Dupuy, Jean-William Blancard, Corinne Salin, Bénédicte Robinson, Derrick R. Renesto, Patricia Tardieux, Isabelle Frénal, Karine Front Cell Infect Microbiol Cellular and Infection Microbiology The Toxoplasma gondii tachyzoite is a singled-cell obligate intracellular parasite responsible for the acute phase of toxoplasmosis. This polarized cell exhibits an apical complex, a hallmark of the phylum Apicomplexa, essential for motility, invasion, and egress from the host cell. Located on the opposite end of the cell is the basal complex, an elaborated cytoskeletal structure that also plays critical roles in the lytic cycle of the parasite, being involved in motility, cell division, constriction and cytokinesis, as well as intravacuolar cell-cell communication. Nevertheless, only a few proteins of this structure have been described and functionally assessed. In this study, we used spatial proteomics to identify new basal complex components (BCC), and in situ imaging, including ultrastructure expansion microscopy, to position them. We thus confirmed the localization of nine BCCs out of the 12 selected candidates and assigned them to different sub-compartments of the basal complex, including two new domains located above the basal ring and below the posterior cup. Their functional investigation revealed that none of these BCCs are essential for parasite growth in vitro. However, one BCC is critical for constricting of the basal complex, likely through direct interaction with the class VI myosin heavy chain J (MyoJ), and for gliding motility. Four other BCCs, including a phosphatase and a guanylate-binding protein, are involved in the formation and/or maintenance of the intravacuolar parasite connection, which is required for the rosette organization and synchronicity of cell division. Frontiers Media S.A. 2022-10-13 /pmc/articles/PMC9613666/ /pubmed/36310866 http://dx.doi.org/10.3389/fcimb.2022.1010038 Text en Copyright © 2022 Roumégous, Abou Hammoud, Fuster, Dupuy, Blancard, Salin, Robinson, Renesto, Tardieux and Frénal https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Cellular and Infection Microbiology
Roumégous, Chloé
Abou Hammoud, Aya
Fuster, Damien
Dupuy, Jean-William
Blancard, Corinne
Salin, Bénédicte
Robinson, Derrick R.
Renesto, Patricia
Tardieux, Isabelle
Frénal, Karine
Identification of new components of the basal pole of Toxoplasma gondii provides novel insights into its molecular organization and functions
title Identification of new components of the basal pole of Toxoplasma gondii provides novel insights into its molecular organization and functions
title_full Identification of new components of the basal pole of Toxoplasma gondii provides novel insights into its molecular organization and functions
title_fullStr Identification of new components of the basal pole of Toxoplasma gondii provides novel insights into its molecular organization and functions
title_full_unstemmed Identification of new components of the basal pole of Toxoplasma gondii provides novel insights into its molecular organization and functions
title_short Identification of new components of the basal pole of Toxoplasma gondii provides novel insights into its molecular organization and functions
title_sort identification of new components of the basal pole of toxoplasma gondii provides novel insights into its molecular organization and functions
topic Cellular and Infection Microbiology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9613666/
https://www.ncbi.nlm.nih.gov/pubmed/36310866
http://dx.doi.org/10.3389/fcimb.2022.1010038
work_keys_str_mv AT roumegouschloe identificationofnewcomponentsofthebasalpoleoftoxoplasmagondiiprovidesnovelinsightsintoitsmolecularorganizationandfunctions
AT abouhammoudaya identificationofnewcomponentsofthebasalpoleoftoxoplasmagondiiprovidesnovelinsightsintoitsmolecularorganizationandfunctions
AT fusterdamien identificationofnewcomponentsofthebasalpoleoftoxoplasmagondiiprovidesnovelinsightsintoitsmolecularorganizationandfunctions
AT dupuyjeanwilliam identificationofnewcomponentsofthebasalpoleoftoxoplasmagondiiprovidesnovelinsightsintoitsmolecularorganizationandfunctions
AT blancardcorinne identificationofnewcomponentsofthebasalpoleoftoxoplasmagondiiprovidesnovelinsightsintoitsmolecularorganizationandfunctions
AT salinbenedicte identificationofnewcomponentsofthebasalpoleoftoxoplasmagondiiprovidesnovelinsightsintoitsmolecularorganizationandfunctions
AT robinsonderrickr identificationofnewcomponentsofthebasalpoleoftoxoplasmagondiiprovidesnovelinsightsintoitsmolecularorganizationandfunctions
AT renestopatricia identificationofnewcomponentsofthebasalpoleoftoxoplasmagondiiprovidesnovelinsightsintoitsmolecularorganizationandfunctions
AT tardieuxisabelle identificationofnewcomponentsofthebasalpoleoftoxoplasmagondiiprovidesnovelinsightsintoitsmolecularorganizationandfunctions
AT frenalkarine identificationofnewcomponentsofthebasalpoleoftoxoplasmagondiiprovidesnovelinsightsintoitsmolecularorganizationandfunctions