Cell biological characterization of the malaria vaccine candidate trophozoite exported protein 1.

In a genome-wide screen for alpha-helical coiled coil motifs aiming at structurally defined vaccine candidates we identified PFF0165c. This protein is exported in the trophozoite stage and was named accordingly Trophozoite exported protein 1 (Tex1). In an extensive preclinical evaluation of its coil...

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Autores principales:	Caroline Kulangara, Samuel Luedin, Olivier Dietz, Sebastian Rusch, Geraldine Frank, Dania Mueller, Mirjam Moser, Andrey V Kajava, Giampietro Corradin, Hans-Peter Beck, Ingrid Felger
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2012
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/0c15e04bb17d487c869937223bbca6d0
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spelling	oai:doaj.org-article:0c15e04bb17d487c869937223bbca6d02021-11-18T08:12:57ZCell biological characterization of the malaria vaccine candidate trophozoite exported protein 1.1932-620310.1371/journal.pone.0046112https://doaj.org/article/0c15e04bb17d487c869937223bbca6d02012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23056243/?tool=EBIhttps://doaj.org/toc/1932-6203In a genome-wide screen for alpha-helical coiled coil motifs aiming at structurally defined vaccine candidates we identified PFF0165c. This protein is exported in the trophozoite stage and was named accordingly Trophozoite exported protein 1 (Tex1). In an extensive preclinical evaluation of its coiled coil peptides Tex1 was identified as promising novel malaria vaccine candidate providing the rational for a comprehensive cell biological characterization of Tex1. Antibodies generated against an intrinsically unstructured N-terminal region of Tex1 and against a coiled coil domain were used to investigate cytological localization, solubility and expression profile. Co-localization experiments revealed that Tex1 is exported across the parasitophorous vacuole membrane and located to Maurer's clefts. Change in location is accompanied by a change in solubility: from a soluble state within the parasite to a membrane-associated state after export to Maurer's clefts. No classical export motifs such as PEXEL, signal sequence/anchor or transmembrane domain was identified for Tex1.Caroline KulangaraSamuel LuedinOlivier DietzSebastian RuschGeraldine FrankDania MuellerMirjam MoserAndrey V KajavaGiampietro CorradinHans-Peter BeckIngrid FelgerPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 7, Iss 10, p e46112 (2012)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Caroline Kulangara Samuel Luedin Olivier Dietz Sebastian Rusch Geraldine Frank Dania Mueller Mirjam Moser Andrey V Kajava Giampietro Corradin Hans-Peter Beck Ingrid Felger Cell biological characterization of the malaria vaccine candidate trophozoite exported protein 1.
description	In a genome-wide screen for alpha-helical coiled coil motifs aiming at structurally defined vaccine candidates we identified PFF0165c. This protein is exported in the trophozoite stage and was named accordingly Trophozoite exported protein 1 (Tex1). In an extensive preclinical evaluation of its coiled coil peptides Tex1 was identified as promising novel malaria vaccine candidate providing the rational for a comprehensive cell biological characterization of Tex1. Antibodies generated against an intrinsically unstructured N-terminal region of Tex1 and against a coiled coil domain were used to investigate cytological localization, solubility and expression profile. Co-localization experiments revealed that Tex1 is exported across the parasitophorous vacuole membrane and located to Maurer's clefts. Change in location is accompanied by a change in solubility: from a soluble state within the parasite to a membrane-associated state after export to Maurer's clefts. No classical export motifs such as PEXEL, signal sequence/anchor or transmembrane domain was identified for Tex1.
format	article
author	Caroline Kulangara Samuel Luedin Olivier Dietz Sebastian Rusch Geraldine Frank Dania Mueller Mirjam Moser Andrey V Kajava Giampietro Corradin Hans-Peter Beck Ingrid Felger
author_facet	Caroline Kulangara Samuel Luedin Olivier Dietz Sebastian Rusch Geraldine Frank Dania Mueller Mirjam Moser Andrey V Kajava Giampietro Corradin Hans-Peter Beck Ingrid Felger
author_sort	Caroline Kulangara
title	Cell biological characterization of the malaria vaccine candidate trophozoite exported protein 1.
title_short	Cell biological characterization of the malaria vaccine candidate trophozoite exported protein 1.
title_full	Cell biological characterization of the malaria vaccine candidate trophozoite exported protein 1.
title_fullStr	Cell biological characterization of the malaria vaccine candidate trophozoite exported protein 1.
title_full_unstemmed	Cell biological characterization of the malaria vaccine candidate trophozoite exported protein 1.
title_sort	cell biological characterization of the malaria vaccine candidate trophozoite exported protein 1.
publisher	Public Library of Science (PLoS)
publishDate	2012
url	https://doaj.org/article/0c15e04bb17d487c869937223bbca6d0
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Cell biological characterization of the malaria vaccine candidate trophozoite exported protein 1.

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