Journal
FEBS LETTERS
Volume 587, Issue 19, Pages 3182-3187Publisher
WILEY
DOI: 10.1016/j.febslet.2013.07.052
Keywords
Malaria; Plasmodium; Glucose; Hexokinase; Hexose transport
Funding
- European Commission project ANTIMAL [018834]
- European Commission project MALSIG [223044]
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To characterise plasmodial glycolysis, we generated two transgenic Plasmodium falciparum lines, one expressing P. falciparum hexokinase (PfHK) tagged with GFP (3D7-PfHK(GFP)) and another overexpressing native PfHK (3D7-PfHK(+)). Contrary to previous reports, we propose that PfHK is cytosolic. The glucose analogue, 2-deoxy-D-glucose (2-DG) was nearly 2-fold less toxic to 3D7-PfHK(+) compared with control parasites, supporting PfHK as a potential drug target. Although PfHK activity was higher in 3D7-PfHK(+), they accumulated phospho-[C-14]2-DG at the same rate as control parasites. Transgenic parasites overexpressing the parasite's glucose transporter (PfHT) accumulated phospho-[C-14]2-DG at a higher rate, consistent with glucose transport limiting glucose entry into glycolysis. (C) 2013 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
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