Plasmodium falciparum FIKK kinase members target distinct components of the erythrocyte membrane.

<h4>Background</h4>Modulation of infected host cells by intracellular pathogens is a prerequisite for successful establishment of infection. In the human malaria parasite Plasmodium falciparum, potential candidates for erythrocyte remodelling include the apicomplexan-specific FIKK kinase...

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Autores principales:	Marta C Nunes, Mami Okada, Christine Scheidig-Benatar, Brian M Cooke, Artur Scherf
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2010
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/61ee41b351864c19ae9fa913aef8b8e8
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spelling	oai:doaj.org-article:61ee41b351864c19ae9fa913aef8b8e82021-12-02T20:19:49ZPlasmodium falciparum FIKK kinase members target distinct components of the erythrocyte membrane.1932-620310.1371/journal.pone.0011747https://doaj.org/article/61ee41b351864c19ae9fa913aef8b8e82010-07-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/20668526/?tool=EBIhttps://doaj.org/toc/1932-6203<h4>Background</h4>Modulation of infected host cells by intracellular pathogens is a prerequisite for successful establishment of infection. In the human malaria parasite Plasmodium falciparum, potential candidates for erythrocyte remodelling include the apicomplexan-specific FIKK kinase family (20 members), several of which have been demonstrated to be transported into the erythrocyte cytoplasm via Maurer's clefts.<h4>Methodology</h4>In the current work, we have knocked out two members of this gene family (Pf fikk7.1 and Pf fikk12), whose products are localized at the inner face of the erythrocyte membrane. Both mutant parasite lines were viable and erythrocytes infected with these parasites showed no detectable alteration in their ability to adhere in vitro to endothelial receptors such as chondroitin sulfate A and CD36. However, we observed sizeable decreases in the rigidity of infected erythrocytes in both knockout lines. Mutant parasites were further analyzed using a phospho-proteomic approach, which revealed distinct phosphorylation profiles in ghost preparations of infected erythrocytes. Knockout parasites showed a significant reduction in the level of phosphorylation of a protein of approximately 80 kDa for FIKK12-KO in trophozoite stage and a large protein of about 300 kDa for FIKK7.1-KO in schizont stage.<h4>Conclusions</h4>Our results suggest that FIKK members phosphorylate different membrane skeleton proteins of the infected erythrocyte in a stage-specific manner, inducing alterations in the mechanical properties of the parasite-infected red blood cell. This suggests that these host cell modifications may contribute to the parasites' survival in the circulation of the human host.Marta C NunesMami OkadaChristine Scheidig-BenatarBrian M CookeArtur ScherfPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 5, Iss 7, p e11747 (2010)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Marta C Nunes Mami Okada Christine Scheidig-Benatar Brian M Cooke Artur Scherf Plasmodium falciparum FIKK kinase members target distinct components of the erythrocyte membrane.
description	<h4>Background</h4>Modulation of infected host cells by intracellular pathogens is a prerequisite for successful establishment of infection. In the human malaria parasite Plasmodium falciparum, potential candidates for erythrocyte remodelling include the apicomplexan-specific FIKK kinase family (20 members), several of which have been demonstrated to be transported into the erythrocyte cytoplasm via Maurer's clefts.<h4>Methodology</h4>In the current work, we have knocked out two members of this gene family (Pf fikk7.1 and Pf fikk12), whose products are localized at the inner face of the erythrocyte membrane. Both mutant parasite lines were viable and erythrocytes infected with these parasites showed no detectable alteration in their ability to adhere in vitro to endothelial receptors such as chondroitin sulfate A and CD36. However, we observed sizeable decreases in the rigidity of infected erythrocytes in both knockout lines. Mutant parasites were further analyzed using a phospho-proteomic approach, which revealed distinct phosphorylation profiles in ghost preparations of infected erythrocytes. Knockout parasites showed a significant reduction in the level of phosphorylation of a protein of approximately 80 kDa for FIKK12-KO in trophozoite stage and a large protein of about 300 kDa for FIKK7.1-KO in schizont stage.<h4>Conclusions</h4>Our results suggest that FIKK members phosphorylate different membrane skeleton proteins of the infected erythrocyte in a stage-specific manner, inducing alterations in the mechanical properties of the parasite-infected red blood cell. This suggests that these host cell modifications may contribute to the parasites' survival in the circulation of the human host.
format	article
author	Marta C Nunes Mami Okada Christine Scheidig-Benatar Brian M Cooke Artur Scherf
author_facet	Marta C Nunes Mami Okada Christine Scheidig-Benatar Brian M Cooke Artur Scherf
author_sort	Marta C Nunes
title	Plasmodium falciparum FIKK kinase members target distinct components of the erythrocyte membrane.
title_short	Plasmodium falciparum FIKK kinase members target distinct components of the erythrocyte membrane.
title_full	Plasmodium falciparum FIKK kinase members target distinct components of the erythrocyte membrane.
title_fullStr	Plasmodium falciparum FIKK kinase members target distinct components of the erythrocyte membrane.
title_full_unstemmed	Plasmodium falciparum FIKK kinase members target distinct components of the erythrocyte membrane.
title_sort	plasmodium falciparum fikk kinase members target distinct components of the erythrocyte membrane.
publisher	Public Library of Science (PLoS)
publishDate	2010
url	https://doaj.org/article/61ee41b351864c19ae9fa913aef8b8e8
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Plasmodium falciparum FIKK kinase members target distinct components of the erythrocyte membrane.

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