Evidence that the <named-content content-type="genus-species">Plasmodium falciparum</named-content> Protein Sortilin Potentially Acts as an Escorter for the Trafficking of the Rhoptry-Associated Membrane Antigen to the Rhoptries

ABSTRACT The rhoptry organelle is critical for the invasion of an erythrocyte by the malaria parasite Plasmodium falciparum. Despite their critical roles, the mechanisms behind their biogenesis are still poorly defined. Our earlier work had suggested that the interaction between the glycosylphosphat...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Stéphanie Hallée, Justin A. Boddey, Alan F. Cowman, Dave Richard
Formato:	article
Lenguaje:	EN
Publicado:	American Society for Microbiology 2018
Materias:	malaria sortilin protein trafficking Microbiology QR1-502
Acceso en línea:	https://doaj.org/article/aa0f0f452c7c44d586f0218801e736c4
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:aa0f0f452c7c44d586f0218801e736c4
record_format	dspace
spelling	oai:doaj.org-article:aa0f0f452c7c44d586f0218801e736c42021-11-15T15:22:01ZEvidence that the <named-content content-type="genus-species">Plasmodium falciparum</named-content> Protein Sortilin Potentially Acts as an Escorter for the Trafficking of the Rhoptry-Associated Membrane Antigen to the Rhoptries10.1128/mSphere.00551-172379-5042https://doaj.org/article/aa0f0f452c7c44d586f0218801e736c42018-02-01T00:00:00Zhttps://journals.asm.org/doi/10.1128/mSphere.00551-17https://doaj.org/toc/2379-5042ABSTRACT The rhoptry organelle is critical for the invasion of an erythrocyte by the malaria parasite Plasmodium falciparum. Despite their critical roles, the mechanisms behind their biogenesis are still poorly defined. Our earlier work had suggested that the interaction between the glycosylphosphatidylinositol (GPI)-anchored rhoptry-associated membrane antigen (RAMA) and the soluble rhoptry-associated protein 1 was involved in the transport of the latter from the Golgi apparatus to the rhoptry. However, how this protein complex could interact with the intracellular trafficking machinery was unknown at this stage. Here we show that the P. falciparum homologue of the transmembrane protein sortilin-VPS10 interacts with regions of RAMA that are sufficient to target a fluorescent reporter to the rhoptries. These results suggest that P. falciparum sortilin (PfSortilin) could potentially act as the escorter for the transport of rhoptry-destined cargo. IMPORTANCE The malaria parasite is a massive burden in several parts of the world. Worryingly, the parasite has become resistant to several of the drugs commonly used to treat the disease, and at this time, there is no commercial vaccine. It is therefore critical to identify new targets for the development of antimalarials. To survive in the human body, the malaria parasite needs to invade red blood cells. For this, it uses a variety of effectors stored in organelles forming a structure called the apical complex. The mechanisms behind how the parasite generates the apical complex are poorly understood. In this study, we present evidence that a transmembrane protein called sortilin potentially acts as an escorter to transport proteins from the Golgi apparatus to the rhoptries, a component of the apical complex. Our study provides new insight into the biogenesis of a critical structure of the malaria parasite.Stéphanie HalléeJustin A. BoddeyAlan F. CowmanDave RichardAmerican Society for Microbiologyarticlemalariasortilinprotein traffickingMicrobiologyQR1-502ENmSphere, Vol 3, Iss 1 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	malaria sortilin protein trafficking Microbiology QR1-502
spellingShingle	malaria sortilin protein trafficking Microbiology QR1-502 Stéphanie Hallée Justin A. Boddey Alan F. Cowman Dave Richard Evidence that the <named-content content-type="genus-species">Plasmodium falciparum</named-content> Protein Sortilin Potentially Acts as an Escorter for the Trafficking of the Rhoptry-Associated Membrane Antigen to the Rhoptries
description	ABSTRACT The rhoptry organelle is critical for the invasion of an erythrocyte by the malaria parasite Plasmodium falciparum. Despite their critical roles, the mechanisms behind their biogenesis are still poorly defined. Our earlier work had suggested that the interaction between the glycosylphosphatidylinositol (GPI)-anchored rhoptry-associated membrane antigen (RAMA) and the soluble rhoptry-associated protein 1 was involved in the transport of the latter from the Golgi apparatus to the rhoptry. However, how this protein complex could interact with the intracellular trafficking machinery was unknown at this stage. Here we show that the P. falciparum homologue of the transmembrane protein sortilin-VPS10 interacts with regions of RAMA that are sufficient to target a fluorescent reporter to the rhoptries. These results suggest that P. falciparum sortilin (PfSortilin) could potentially act as the escorter for the transport of rhoptry-destined cargo. IMPORTANCE The malaria parasite is a massive burden in several parts of the world. Worryingly, the parasite has become resistant to several of the drugs commonly used to treat the disease, and at this time, there is no commercial vaccine. It is therefore critical to identify new targets for the development of antimalarials. To survive in the human body, the malaria parasite needs to invade red blood cells. For this, it uses a variety of effectors stored in organelles forming a structure called the apical complex. The mechanisms behind how the parasite generates the apical complex are poorly understood. In this study, we present evidence that a transmembrane protein called sortilin potentially acts as an escorter to transport proteins from the Golgi apparatus to the rhoptries, a component of the apical complex. Our study provides new insight into the biogenesis of a critical structure of the malaria parasite.
format	article
author	Stéphanie Hallée Justin A. Boddey Alan F. Cowman Dave Richard
author_facet	Stéphanie Hallée Justin A. Boddey Alan F. Cowman Dave Richard
author_sort	Stéphanie Hallée
title	Evidence that the <named-content content-type="genus-species">Plasmodium falciparum</named-content> Protein Sortilin Potentially Acts as an Escorter for the Trafficking of the Rhoptry-Associated Membrane Antigen to the Rhoptries
title_short	Evidence that the <named-content content-type="genus-species">Plasmodium falciparum</named-content> Protein Sortilin Potentially Acts as an Escorter for the Trafficking of the Rhoptry-Associated Membrane Antigen to the Rhoptries
title_full	Evidence that the <named-content content-type="genus-species">Plasmodium falciparum</named-content> Protein Sortilin Potentially Acts as an Escorter for the Trafficking of the Rhoptry-Associated Membrane Antigen to the Rhoptries
title_fullStr	Evidence that the <named-content content-type="genus-species">Plasmodium falciparum</named-content> Protein Sortilin Potentially Acts as an Escorter for the Trafficking of the Rhoptry-Associated Membrane Antigen to the Rhoptries
title_full_unstemmed	Evidence that the <named-content content-type="genus-species">Plasmodium falciparum</named-content> Protein Sortilin Potentially Acts as an Escorter for the Trafficking of the Rhoptry-Associated Membrane Antigen to the Rhoptries
title_sort	evidence that the <named-content content-type="genus-species">plasmodium falciparum</named-content> protein sortilin potentially acts as an escorter for the trafficking of the rhoptry-associated membrane antigen to the rhoptries
publisher	American Society for Microbiology
publishDate	2018
url	https://doaj.org/article/aa0f0f452c7c44d586f0218801e736c4
work_keys_str_mv	AT stephaniehallee evidencethatthenamedcontentcontenttypegenusspeciesplasmodiumfalciparumnamedcontentproteinsortilinpotentiallyactsasanescorterforthetraffickingoftherhoptryassociatedmembraneantigentotherhoptries AT justinaboddey evidencethatthenamedcontentcontenttypegenusspeciesplasmodiumfalciparumnamedcontentproteinsortilinpotentiallyactsasanescorterforthetraffickingoftherhoptryassociatedmembraneantigentotherhoptries AT alanfcowman evidencethatthenamedcontentcontenttypegenusspeciesplasmodiumfalciparumnamedcontentproteinsortilinpotentiallyactsasanescorterforthetraffickingoftherhoptryassociatedmembraneantigentotherhoptries AT daverichard evidencethatthenamedcontentcontenttypegenusspeciesplasmodiumfalciparumnamedcontentproteinsortilinpotentiallyactsasanescorterforthetraffickingoftherhoptryassociatedmembraneantigentotherhoptries
_version_	1718428089850003456

Evidence that the <named-content content-type="genus-species">Plasmodium falciparum</named-content> Protein Sortilin Potentially Acts as an Escorter for the Trafficking of the Rhoptry-Associated Membrane Antigen to the Rhoptries

Ejemplares similares