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Identification and characterisation of a phospholipid scramblase in the malaria parasite Plasmodium falciparum.
Haase, Silvia; Condron, Melanie; Miller, David; Cherkaoui, Dounia; Jordan, Sarah; Gulbis, Jacqueline M; Baum, Jake.
Afiliación
  • Haase S; Department of Life Sciences, Imperial College London, Sir Alexander Fleming Building, Exhibition Road, South Kensington, London, UK. Electronic address: silvia.haase@crick.ac.uk.
  • Condron M; Division of Infection and Immunity, The Walter and Eliza Hall Institute of Medical Research, Melbourne, Victoria, Australia.
  • Miller D; Division of Structural Biology, The Walter and Eliza Hall Institute of Medical Research, Melbourne, Victoria, Australia.
  • Cherkaoui D; Department of Life Sciences, Imperial College London, Sir Alexander Fleming Building, Exhibition Road, South Kensington, London, UK.
  • Jordan S; Department of Life Sciences, Imperial College London, Sir Alexander Fleming Building, Exhibition Road, South Kensington, London, UK.
  • Gulbis JM; Division of Structural Biology, The Walter and Eliza Hall Institute of Medical Research, Melbourne, Victoria, Australia; Department of Medical Biology, The University of Melbourne, Melbourne, Victoria, Australia.
  • Baum J; Department of Life Sciences, Imperial College London, Sir Alexander Fleming Building, Exhibition Road, South Kensington, London, UK. Electronic address: jake.baum@imperial.ac.uk.
Mol Biochem Parasitol ; 243: 111374, 2021 05.
Article en En | MEDLINE | ID: mdl-33974939
Recent studies highlight the emerging role of lipids as important messengers in malaria parasite biology. In an attempt to identify interacting proteins and regulators of these dynamic and versatile molecules, we hypothesised the involvement of phospholipid translocases and their substrates in the infection of the host erythrocyte by the malaria parasite Plasmodium spp. Here, using a data base searching approach of the Plasmodium Genomics Resources (www.plasmodb.org), we have identified a putative phospholipid (PL) scramblase in P. falciparum (PfPLSCR) that is conserved across the genus and in closely related unicellular algae. By reconstituting recombinant PfPLSCR into liposomes, we demonstrate metal ion dependent PL translocase activity and substrate preference, confirming PfPLSCR as a bona fide scramblase. We show that PfPLSCR is expressed during asexual and sexual parasite development, localising to different membranous compartments of the parasite throughout the intra-erythrocytic life cycle. Two different gene knockout approaches, however, suggest that PfPLSCR is not essential for erythrocyte invasion and asexual parasite development, pointing towards a possible role in other stages of the parasite life cycle.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Plasmodium falciparum / Proteínas Protozoarias / Proteínas de Transferencia de Fosfolípidos Tipo de estudio: Diagnostic_studies Límite: Humans Idioma: En Revista: Mol Biochem Parasitol Año: 2021 Tipo del documento: Article Pais de publicación: Países Bajos
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Plasmodium falciparum / Proteínas Protozoarias / Proteínas de Transferencia de Fosfolípidos Tipo de estudio: Diagnostic_studies Límite: Humans Idioma: En Revista: Mol Biochem Parasitol Año: 2021 Tipo del documento: Article Pais de publicación: Países Bajos