1. Identification of new components of the basal pole of Toxoplasma gondii provides novel insights into its molecular organization and functions
- Author
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Chloé Roumégous, Aya Abou Hammoud, Damien Fuster, Jean-William Dupuy, Corinne Blancard, Bénédicte Salin, Derrick R. Robinson, Patricia Renesto, Isabelle Tardieux, Karine Frénal, Microbiologie Fondamentale et Pathogénicité (MFP), Université Bordeaux Segalen - Bordeaux 2-Centre National de la Recherche Scientifique (CNRS), Plateforme Protéome [Bordeaux], Centre Génomique Fonctionnelle Bordeaux [Bordeaux] (CGFB), Institut Polytechnique de Bordeaux-Université de Bordeaux Ségalen [Bordeaux 2]-Institut Polytechnique de Bordeaux-Université de Bordeaux Ségalen [Bordeaux 2], Institut de biochimie et génétique cellulaires (IBGC), Institute for Advanced Biosciences / Institut pour l'Avancée des Biosciences (Grenoble) (IAB), Centre Hospitalier Universitaire [Grenoble] (CHU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Etablissement français du sang - Auvergne-Rhône-Alpes (EFS)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes (UGA), ANR-11-LABX-0024, and Frenal, Karine
- Subjects
Microbiology (medical) ,[SDV]Life Sciences [q-bio] ,Immunology ,Protozoan Proteins ,Myosin ,Toxoplasma gondii ,cytoskeleton ,Microbiology ,[SDV] Life Sciences [q-bio] ,Infectious Diseases ,Humans ,[SDV.MP.PAR]Life Sciences [q-bio]/Microbiology and Parasitology/Parasitology ,Toxoplasma ,Toxoplasmosis ,Cell Division ,[SDV.MP.PAR] Life Sciences [q-bio]/Microbiology and Parasitology/Parasitology - Abstract
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.
- Published
- 2022
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