Theileria equi claudin like apicomplexan microneme protein contains neutralization-sensitive epitopes and interacts with components of the equine erythrocyte membrane skeleton

Abstract Theileria equi is a widely distributed apicomplexan parasite that causes severe hemolytic anemia in equid species. There is currently no effective vaccine for control of the parasite and understanding the mechanism that T. equi utilizes to invade host cells may be crucial for vaccine develo...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Cynthia K. Onzere, Lindsay M. Fry, Richard P. Bishop, Marta G. Silva, Reginaldo G. Bastos, Donald P. Knowles, Carlos E. Suarez
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/ccc01b8ea51445b3b6b80fe9d65346bd
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:ccc01b8ea51445b3b6b80fe9d65346bd
record_format	dspace
spelling	oai:doaj.org-article:ccc01b8ea51445b3b6b80fe9d65346bd2021-12-02T16:55:34ZTheileria equi claudin like apicomplexan microneme protein contains neutralization-sensitive epitopes and interacts with components of the equine erythrocyte membrane skeleton10.1038/s41598-021-88902-42045-2322https://doaj.org/article/ccc01b8ea51445b3b6b80fe9d65346bd2021-04-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-88902-4https://doaj.org/toc/2045-2322Abstract Theileria equi is a widely distributed apicomplexan parasite that causes severe hemolytic anemia in equid species. There is currently no effective vaccine for control of the parasite and understanding the mechanism that T. equi utilizes to invade host cells may be crucial for vaccine development. Unlike most apicomplexan species studied to date, the role of micronemes in T. equi invasion of host cells is unknown. We therefore assessed the role of the T. equi claudin-like apicomplexan microneme protein (CLAMP) in the invasion of equine erythrocytes as a first step towards understanding the role of this organelle in the parasite. Our findings show that CLAMP is expressed in the merozoite and intra-erythrocytic developmental stages of T. equi and in vitro neutralization experiments suggest that the protein is involved in erythrocyte invasion. Proteomic analyses indicate that CLAMP interacts with the equine erythrocyte α-and β- spectrin chains in the initial stages of T. equi invasion and maintains these interactions while also associating with the anion-exchange protein, tropomyosin 3, band 4.1 and cytoplasmic actin 1 after invasion. Additionally, serological analyses show that T. equi-infected horses mount robust antibody responses against CLAMP indicating that the protein is immunogenic and therefore represents a potential vaccine candidate.Cynthia K. OnzereLindsay M. FryRichard P. BishopMarta G. SilvaReginaldo G. BastosDonald P. KnowlesCarlos E. SuarezNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-13 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Cynthia K. Onzere Lindsay M. Fry Richard P. Bishop Marta G. Silva Reginaldo G. Bastos Donald P. Knowles Carlos E. Suarez Theileria equi claudin like apicomplexan microneme protein contains neutralization-sensitive epitopes and interacts with components of the equine erythrocyte membrane skeleton
description	Abstract Theileria equi is a widely distributed apicomplexan parasite that causes severe hemolytic anemia in equid species. There is currently no effective vaccine for control of the parasite and understanding the mechanism that T. equi utilizes to invade host cells may be crucial for vaccine development. Unlike most apicomplexan species studied to date, the role of micronemes in T. equi invasion of host cells is unknown. We therefore assessed the role of the T. equi claudin-like apicomplexan microneme protein (CLAMP) in the invasion of equine erythrocytes as a first step towards understanding the role of this organelle in the parasite. Our findings show that CLAMP is expressed in the merozoite and intra-erythrocytic developmental stages of T. equi and in vitro neutralization experiments suggest that the protein is involved in erythrocyte invasion. Proteomic analyses indicate that CLAMP interacts with the equine erythrocyte α-and β- spectrin chains in the initial stages of T. equi invasion and maintains these interactions while also associating with the anion-exchange protein, tropomyosin 3, band 4.1 and cytoplasmic actin 1 after invasion. Additionally, serological analyses show that T. equi-infected horses mount robust antibody responses against CLAMP indicating that the protein is immunogenic and therefore represents a potential vaccine candidate.
format	article
author	Cynthia K. Onzere Lindsay M. Fry Richard P. Bishop Marta G. Silva Reginaldo G. Bastos Donald P. Knowles Carlos E. Suarez
author_facet	Cynthia K. Onzere Lindsay M. Fry Richard P. Bishop Marta G. Silva Reginaldo G. Bastos Donald P. Knowles Carlos E. Suarez
author_sort	Cynthia K. Onzere
title	Theileria equi claudin like apicomplexan microneme protein contains neutralization-sensitive epitopes and interacts with components of the equine erythrocyte membrane skeleton
title_short	Theileria equi claudin like apicomplexan microneme protein contains neutralization-sensitive epitopes and interacts with components of the equine erythrocyte membrane skeleton
title_full	Theileria equi claudin like apicomplexan microneme protein contains neutralization-sensitive epitopes and interacts with components of the equine erythrocyte membrane skeleton
title_fullStr	Theileria equi claudin like apicomplexan microneme protein contains neutralization-sensitive epitopes and interacts with components of the equine erythrocyte membrane skeleton
title_full_unstemmed	Theileria equi claudin like apicomplexan microneme protein contains neutralization-sensitive epitopes and interacts with components of the equine erythrocyte membrane skeleton
title_sort	theileria equi claudin like apicomplexan microneme protein contains neutralization-sensitive epitopes and interacts with components of the equine erythrocyte membrane skeleton
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/ccc01b8ea51445b3b6b80fe9d65346bd
work_keys_str_mv	AT cynthiakonzere theileriaequiclaudinlikeapicomplexanmicronemeproteincontainsneutralizationsensitiveepitopesandinteractswithcomponentsoftheequineerythrocytemembraneskeleton AT lindsaymfry theileriaequiclaudinlikeapicomplexanmicronemeproteincontainsneutralizationsensitiveepitopesandinteractswithcomponentsoftheequineerythrocytemembraneskeleton AT richardpbishop theileriaequiclaudinlikeapicomplexanmicronemeproteincontainsneutralizationsensitiveepitopesandinteractswithcomponentsoftheequineerythrocytemembraneskeleton AT martagsilva theileriaequiclaudinlikeapicomplexanmicronemeproteincontainsneutralizationsensitiveepitopesandinteractswithcomponentsoftheequineerythrocytemembraneskeleton AT reginaldogbastos theileriaequiclaudinlikeapicomplexanmicronemeproteincontainsneutralizationsensitiveepitopesandinteractswithcomponentsoftheequineerythrocytemembraneskeleton AT donaldpknowles theileriaequiclaudinlikeapicomplexanmicronemeproteincontainsneutralizationsensitiveepitopesandinteractswithcomponentsoftheequineerythrocytemembraneskeleton AT carlosesuarez theileriaequiclaudinlikeapicomplexanmicronemeproteincontainsneutralizationsensitiveepitopesandinteractswithcomponentsoftheequineerythrocytemembraneskeleton
_version_	1718382828062769152

Theileria equi claudin like apicomplexan microneme protein contains neutralization-sensitive epitopes and interacts with components of the equine erythrocyte membrane skeleton

Ejemplares similares