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A lipid-binding protein mediates rhoptry discharge and invasion in Plasmodium falciparum and Toxoplasma gondii parasites

Members of the Apicomplexa phylum, including Plasmodium and Toxoplasma, have two types of secretory organelles (micronemes and rhoptries) whose sequential release is essential for invasion and the intracellular lifestyle of these eukaryotes. During invasion, rhoptries inject an array of invasion and...

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Autores principales: Suarez, Catherine, Lentini, Gaëlle, Ramaswamy, Raghavendran, Maynadier, Marjorie, Aquilini, Eleonora, Berry-Sterkers, Laurence, Cipriano, Michael, Chen, Allan L., Bradley, Peter, Striepen, Boris, Boulanger, Martin J., Lebrun, Maryse
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6731292/
https://www.ncbi.nlm.nih.gov/pubmed/31492901
http://dx.doi.org/10.1038/s41467-019-11979-z
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author Suarez, Catherine
Lentini, Gaëlle
Ramaswamy, Raghavendran
Maynadier, Marjorie
Aquilini, Eleonora
Berry-Sterkers, Laurence
Cipriano, Michael
Chen, Allan L.
Bradley, Peter
Striepen, Boris
Boulanger, Martin J.
Lebrun, Maryse
author_facet Suarez, Catherine
Lentini, Gaëlle
Ramaswamy, Raghavendran
Maynadier, Marjorie
Aquilini, Eleonora
Berry-Sterkers, Laurence
Cipriano, Michael
Chen, Allan L.
Bradley, Peter
Striepen, Boris
Boulanger, Martin J.
Lebrun, Maryse
author_sort Suarez, Catherine
collection PubMed
description Members of the Apicomplexa phylum, including Plasmodium and Toxoplasma, have two types of secretory organelles (micronemes and rhoptries) whose sequential release is essential for invasion and the intracellular lifestyle of these eukaryotes. During invasion, rhoptries inject an array of invasion and virulence factors into the cytoplasm of the host cell, but the molecular mechanism mediating rhoptry exocytosis is unknown. Here we identify a set of parasite specific proteins, termed rhoptry apical surface proteins (RASP) that cap the extremity of the rhoptry. Depletion of RASP2 results in loss of rhoptry secretion and completely blocks parasite invasion and therefore parasite proliferation in both Toxoplasma and Plasmodium. Recombinant RASP2 binds charged lipids and likely contributes to assembling the machinery that docks/primes the rhoptry to the plasma membrane prior to fusion. This study provides important mechanistic insight into a parasite specific exocytic pathway, essential for the establishment of infection.
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spelling pubmed-67312922019-09-09 A lipid-binding protein mediates rhoptry discharge and invasion in Plasmodium falciparum and Toxoplasma gondii parasites Suarez, Catherine Lentini, Gaëlle Ramaswamy, Raghavendran Maynadier, Marjorie Aquilini, Eleonora Berry-Sterkers, Laurence Cipriano, Michael Chen, Allan L. Bradley, Peter Striepen, Boris Boulanger, Martin J. Lebrun, Maryse Nat Commun Article Members of the Apicomplexa phylum, including Plasmodium and Toxoplasma, have two types of secretory organelles (micronemes and rhoptries) whose sequential release is essential for invasion and the intracellular lifestyle of these eukaryotes. During invasion, rhoptries inject an array of invasion and virulence factors into the cytoplasm of the host cell, but the molecular mechanism mediating rhoptry exocytosis is unknown. Here we identify a set of parasite specific proteins, termed rhoptry apical surface proteins (RASP) that cap the extremity of the rhoptry. Depletion of RASP2 results in loss of rhoptry secretion and completely blocks parasite invasion and therefore parasite proliferation in both Toxoplasma and Plasmodium. Recombinant RASP2 binds charged lipids and likely contributes to assembling the machinery that docks/primes the rhoptry to the plasma membrane prior to fusion. This study provides important mechanistic insight into a parasite specific exocytic pathway, essential for the establishment of infection. Nature Publishing Group UK 2019-09-06 /pmc/articles/PMC6731292/ /pubmed/31492901 http://dx.doi.org/10.1038/s41467-019-11979-z Text en © The Author(s) 2019 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Article
Suarez, Catherine
Lentini, Gaëlle
Ramaswamy, Raghavendran
Maynadier, Marjorie
Aquilini, Eleonora
Berry-Sterkers, Laurence
Cipriano, Michael
Chen, Allan L.
Bradley, Peter
Striepen, Boris
Boulanger, Martin J.
Lebrun, Maryse
A lipid-binding protein mediates rhoptry discharge and invasion in Plasmodium falciparum and Toxoplasma gondii parasites
title A lipid-binding protein mediates rhoptry discharge and invasion in Plasmodium falciparum and Toxoplasma gondii parasites
title_full A lipid-binding protein mediates rhoptry discharge and invasion in Plasmodium falciparum and Toxoplasma gondii parasites
title_fullStr A lipid-binding protein mediates rhoptry discharge and invasion in Plasmodium falciparum and Toxoplasma gondii parasites
title_full_unstemmed A lipid-binding protein mediates rhoptry discharge and invasion in Plasmodium falciparum and Toxoplasma gondii parasites
title_short A lipid-binding protein mediates rhoptry discharge and invasion in Plasmodium falciparum and Toxoplasma gondii parasites
title_sort lipid-binding protein mediates rhoptry discharge and invasion in plasmodium falciparum and toxoplasma gondii parasites
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6731292/
https://www.ncbi.nlm.nih.gov/pubmed/31492901
http://dx.doi.org/10.1038/s41467-019-11979-z
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