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The BCC7 Protein Contributes to the Toxoplasma Basal Pole by Interfacing between the MyoC Motor and the IMC Membrane Network

T. gondii is a eukaryotic parasite that has evolved a stage called tachyzoite which multiplies in host cells by producing two daughter cells internally. These nascent tachyzoites bud off their mother and repeat the division process until the expanding progenies escape to settle and multiply in other...

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Autores principales: Vigetti, Luis, Labouré, Tatiana, Roumégous, Chloé, Cannella, Dominique, Touquet, Bastien, Mayer, Claudine, Couté, Yohann, Frénal, Karine, Tardieux, Isabelle, Renesto, Patricia
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9181098/
https://www.ncbi.nlm.nih.gov/pubmed/35682673
http://dx.doi.org/10.3390/ijms23115995
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author Vigetti, Luis
Labouré, Tatiana
Roumégous, Chloé
Cannella, Dominique
Touquet, Bastien
Mayer, Claudine
Couté, Yohann
Frénal, Karine
Tardieux, Isabelle
Renesto, Patricia
author_facet Vigetti, Luis
Labouré, Tatiana
Roumégous, Chloé
Cannella, Dominique
Touquet, Bastien
Mayer, Claudine
Couté, Yohann
Frénal, Karine
Tardieux, Isabelle
Renesto, Patricia
author_sort Vigetti, Luis
collection PubMed
description T. gondii is a eukaryotic parasite that has evolved a stage called tachyzoite which multiplies in host cells by producing two daughter cells internally. These nascent tachyzoites bud off their mother and repeat the division process until the expanding progenies escape to settle and multiply in other host cells. Over these intra- and extra-cellular phases, the tachyzoite maintains an essential apicobasal polarity that emerges through a unique bidirectional budding process of the elongating cells. This process requires the assembly of several molecular complexes that, at the nascent pole, encompass structural and myosin motor elements. To characterize a recently identified basal pole marker named BCC7 with respect to the posterior myosin J and myosin C motors, we used conventional biochemistry as well as advanced proteomic and in silico analysis in conjunction with live and super resolution microscopy of transgenic fluorescent tachyzoites. We document that BCC7 forms a ribbed ring below which myosin C motor entities distribute regularly. In addition, we identified—among 13 BCC7 putative partners—two novel and five known members of the inner membrane complex (IMC) family which ends at the apical side of the ring. Therefore, BCC7 could assist the stabilization of the IMC plaques and contribute to the parasite biomechanical properties.
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spelling pubmed-91810982022-06-10 The BCC7 Protein Contributes to the Toxoplasma Basal Pole by Interfacing between the MyoC Motor and the IMC Membrane Network Vigetti, Luis Labouré, Tatiana Roumégous, Chloé Cannella, Dominique Touquet, Bastien Mayer, Claudine Couté, Yohann Frénal, Karine Tardieux, Isabelle Renesto, Patricia Int J Mol Sci Article T. gondii is a eukaryotic parasite that has evolved a stage called tachyzoite which multiplies in host cells by producing two daughter cells internally. These nascent tachyzoites bud off their mother and repeat the division process until the expanding progenies escape to settle and multiply in other host cells. Over these intra- and extra-cellular phases, the tachyzoite maintains an essential apicobasal polarity that emerges through a unique bidirectional budding process of the elongating cells. This process requires the assembly of several molecular complexes that, at the nascent pole, encompass structural and myosin motor elements. To characterize a recently identified basal pole marker named BCC7 with respect to the posterior myosin J and myosin C motors, we used conventional biochemistry as well as advanced proteomic and in silico analysis in conjunction with live and super resolution microscopy of transgenic fluorescent tachyzoites. We document that BCC7 forms a ribbed ring below which myosin C motor entities distribute regularly. In addition, we identified—among 13 BCC7 putative partners—two novel and five known members of the inner membrane complex (IMC) family which ends at the apical side of the ring. Therefore, BCC7 could assist the stabilization of the IMC plaques and contribute to the parasite biomechanical properties. MDPI 2022-05-26 /pmc/articles/PMC9181098/ /pubmed/35682673 http://dx.doi.org/10.3390/ijms23115995 Text en © 2022 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
Vigetti, Luis
Labouré, Tatiana
Roumégous, Chloé
Cannella, Dominique
Touquet, Bastien
Mayer, Claudine
Couté, Yohann
Frénal, Karine
Tardieux, Isabelle
Renesto, Patricia
The BCC7 Protein Contributes to the Toxoplasma Basal Pole by Interfacing between the MyoC Motor and the IMC Membrane Network
title The BCC7 Protein Contributes to the Toxoplasma Basal Pole by Interfacing between the MyoC Motor and the IMC Membrane Network
title_full The BCC7 Protein Contributes to the Toxoplasma Basal Pole by Interfacing between the MyoC Motor and the IMC Membrane Network
title_fullStr The BCC7 Protein Contributes to the Toxoplasma Basal Pole by Interfacing between the MyoC Motor and the IMC Membrane Network
title_full_unstemmed The BCC7 Protein Contributes to the Toxoplasma Basal Pole by Interfacing between the MyoC Motor and the IMC Membrane Network
title_short The BCC7 Protein Contributes to the Toxoplasma Basal Pole by Interfacing between the MyoC Motor and the IMC Membrane Network
title_sort bcc7 protein contributes to the toxoplasma basal pole by interfacing between the myoc motor and the imc membrane network
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9181098/
https://www.ncbi.nlm.nih.gov/pubmed/35682673
http://dx.doi.org/10.3390/ijms23115995
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