Characterization of the small exported Plasmodium falciparum membrane protein SEMP1.

Survival and virulence of the human malaria parasite Plasmodium falciparum during the blood stage of infection critically depend on extensive host cell refurbishments mediated through export of numerous parasite proteins into the host cell. The parasite-derived membranous structures called Maurer�...

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Autores principales:	Olivier Dietz, Sebastian Rusch, Françoise Brand, Esther Mundwiler-Pachlatko, Annette Gaida, Till Voss, Hans-Peter Beck
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2014
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/8c60295cd75345d49254eb0fc1f67ebb
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spelling	oai:doaj.org-article:8c60295cd75345d49254eb0fc1f67ebb2021-11-25T06:07:05ZCharacterization of the small exported Plasmodium falciparum membrane protein SEMP1.1932-620310.1371/journal.pone.0103272https://doaj.org/article/8c60295cd75345d49254eb0fc1f67ebb2014-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/25062022/?tool=EBIhttps://doaj.org/toc/1932-6203Survival and virulence of the human malaria parasite Plasmodium falciparum during the blood stage of infection critically depend on extensive host cell refurbishments mediated through export of numerous parasite proteins into the host cell. The parasite-derived membranous structures called Maurer's clefts (MC) play an important role in protein trafficking from the parasite to the red blood cell membrane. However, their specific function has yet to be determined. We identified and characterized a new MC membrane protein, termed small exported membrane protein 1 (SEMP1). Upon invasion it is exported into the RBC cytosol where it inserts into the MCs before it is partly translocated to the RBC membrane. Using conventional and conditional loss-of-function approaches we showed that SEMP1 is not essential for parasite survival, gametocytogenesis, or PfEMP1 export under culture conditions. Co-IP experiments identified several potential interaction partners, including REX1 and other membrane-associated proteins that were confirmed to co-localize with SEMP1 at MCs. Transcriptome analysis further showed that expression of a number of exported parasite proteins was up-regulated in SEMP1-depleted parasites. By using Co-IP and transcriptome analysis for functional characterization of an exported parasite protein we provide a new starting point for further detailed dissection and characterisation of MC-associated protein complexes.Olivier DietzSebastian RuschFrançoise BrandEsther Mundwiler-PachlatkoAnnette GaidaTill VossHans-Peter BeckPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 9, Iss 7, p e103272 (2014)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Olivier Dietz Sebastian Rusch Françoise Brand Esther Mundwiler-Pachlatko Annette Gaida Till Voss Hans-Peter Beck Characterization of the small exported Plasmodium falciparum membrane protein SEMP1.
description	Survival and virulence of the human malaria parasite Plasmodium falciparum during the blood stage of infection critically depend on extensive host cell refurbishments mediated through export of numerous parasite proteins into the host cell. The parasite-derived membranous structures called Maurer's clefts (MC) play an important role in protein trafficking from the parasite to the red blood cell membrane. However, their specific function has yet to be determined. We identified and characterized a new MC membrane protein, termed small exported membrane protein 1 (SEMP1). Upon invasion it is exported into the RBC cytosol where it inserts into the MCs before it is partly translocated to the RBC membrane. Using conventional and conditional loss-of-function approaches we showed that SEMP1 is not essential for parasite survival, gametocytogenesis, or PfEMP1 export under culture conditions. Co-IP experiments identified several potential interaction partners, including REX1 and other membrane-associated proteins that were confirmed to co-localize with SEMP1 at MCs. Transcriptome analysis further showed that expression of a number of exported parasite proteins was up-regulated in SEMP1-depleted parasites. By using Co-IP and transcriptome analysis for functional characterization of an exported parasite protein we provide a new starting point for further detailed dissection and characterisation of MC-associated protein complexes.
format	article
author	Olivier Dietz Sebastian Rusch Françoise Brand Esther Mundwiler-Pachlatko Annette Gaida Till Voss Hans-Peter Beck
author_facet	Olivier Dietz Sebastian Rusch Françoise Brand Esther Mundwiler-Pachlatko Annette Gaida Till Voss Hans-Peter Beck
author_sort	Olivier Dietz
title	Characterization of the small exported Plasmodium falciparum membrane protein SEMP1.
title_short	Characterization of the small exported Plasmodium falciparum membrane protein SEMP1.
title_full	Characterization of the small exported Plasmodium falciparum membrane protein SEMP1.
title_fullStr	Characterization of the small exported Plasmodium falciparum membrane protein SEMP1.
title_full_unstemmed	Characterization of the small exported Plasmodium falciparum membrane protein SEMP1.
title_sort	characterization of the small exported plasmodium falciparum membrane protein semp1.
publisher	Public Library of Science (PLoS)
publishDate	2014
url	https://doaj.org/article/8c60295cd75345d49254eb0fc1f67ebb
work_keys_str_mv	AT olivierdietz characterizationofthesmallexportedplasmodiumfalciparummembraneproteinsemp1 AT sebastianrusch characterizationofthesmallexportedplasmodiumfalciparummembraneproteinsemp1 AT francoisebrand characterizationofthesmallexportedplasmodiumfalciparummembraneproteinsemp1 AT esthermundwilerpachlatko characterizationofthesmallexportedplasmodiumfalciparummembraneproteinsemp1 AT annettegaida characterizationofthesmallexportedplasmodiumfalciparummembraneproteinsemp1 AT tillvoss characterizationofthesmallexportedplasmodiumfalciparummembraneproteinsemp1 AT hanspeterbeck characterizationofthesmallexportedplasmodiumfalciparummembraneproteinsemp1
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Characterization of the small exported Plasmodium falciparum membrane protein SEMP1.

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