Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 285, Issue 27, Pages 20827-20833Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M110.118489
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Funding
- National Institutes of Health through the NIAID [AI51507]
- Department of Defense [PR033005]
- Burroughs Wellcome Fund
- Australian Research Council
- National Health and Medical Research Council
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The survival and proliferation of the obligate intracellular malaria parasite Plasmodium falciparum require salvage of essential purines from the host. Genetic studies have previously shown that the parasite plasma membrane purine permease, PfNT1, plays an essential function in the transport of all naturally occurring purine nucleosides and nucleobases across the parasite plasma membrane. Here, we describe an intracellular permease, PfNT2. PfNT2 is, like PfNT1, a member of the equilibrative nucleoside transporter family. Confocal and immunoelectron microscopic analyses of transgenic parasites harboring green fluorescent protein- or hemagglutinin-tagged PfNT2 demonstrated endoplasmic reticulum localization. This localization was confirmed by colocalization with the endoplasmic reticulum marker PfBiP. Using yeast as a surrogate system, we show that targeting PfNT2 to the plasma membrane of fui1 Delta cells lacking the plasma membrane nucleoside transporter Fui1 confers sensitivity to the toxic nucleoside analog 5-fluorouridine. This study provides the first evidence of an intracellular purine permease in apicomplexan parasites and suggests a novel biological function for the parasite endoplasmic reticulum during malaria infection.
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