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Please use this identifier to cite or link to this item: http://hdl.handle.net/10204/4354

Title: PfPI3K, a Phosphatidylinsoitol-3 kinase in Plasmodium falciparum, is exported to the host erythrocyte and is involved in hemoglobin trafficking
Authors: Vaid, A
Ranjan, R
Verma, G
Smythe, WA
Hoppe, HC
Sharma, P
Keywords: Red cells
Iron
Polyphosphorylated phosphoinositides
Erythropoiesis
Eukaryotic cells
Plasmodium falciparum
Hemoglobi
Issue Date: Mar-2010
Publisher: American Society of Hematology
Citation: Vaid, A, Ranjan, R, Verma, G et al. 2010. PfPI3K, a Phosphatidylinsoitol-3 kinase in Plasmodium falciparum, is exported to the host erythrocyte and is involved in hemoglobin trafficking. Blood, Vol. 115(12), pp 2500-2507
Abstract: phosphorylated phosphoinositides (PIPs) are potent second messengers, which trigger a wide variety of signaling and trafficking events in most eukaryotic cells. However, the role and metabolism of PIPs in malaria parasite Plasmodium have remained largely unexplored. Our present studies suggest that PfPI3K, a novel phosphatidylinositol-3-kinase (PI3K) in Plasmodium falciparum, is exported to the host erythrocyte by the parasite in an active form. PfPI3K is a versatile enzyme as it can generate various 3'-phosphorylated PIPs. In the parasite, PfPI3K was localized in vesicular compartments near the membrane and in its food vacuole. PI3K inhibitors wortmannin and LY294002 were effective against PfPI3K and were used to study PfPI3K function. We found that PfPI3K is involved in endocytosis from the host and trafficking of hemoglobin in the parasite. The inhibition of PfPI3K resulted in entrapment of hemoglobin in vesicles in the parasite cytoplasm, which prevented its transport to the food vacuole, the site of hemoglobin catabolism. As a result, hemoglobin digestion, which is a source of amino acids necessary for parasite growth, was attenuated and caused the inhibition of parasite growth.
Description: Copyright: 2010 American Society of Hematology. This is the author's Pre-print Version. The definitive version is published in Blood, Vol. 115(12), pp 2500-2507
URI: http://hdl.handle.net/10204/4354
Appears in Collections:Microbial expression systems
Systems biology
General science, engineering & technology

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