Identity of a Plasmodium lactate/H+ symporter structurally unrelated to human transporters

Binghua Wu, Janis Rambow, Sinja Bock, Julia Holm-Bertelsen, Marie Wiechert, Alexandra Blancke Soares, Tobias Spielmann and Eric Beitz ()
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Binghua Wu: Pharmaceutical Institute, Christian-Albrechts-University of Kiel
Janis Rambow: Pharmaceutical Institute, Christian-Albrechts-University of Kiel
Sinja Bock: Pharmaceutical Institute, Christian-Albrechts-University of Kiel
Julia Holm-Bertelsen: Pharmaceutical Institute, Christian-Albrechts-University of Kiel
Marie Wiechert: Pharmaceutical Institute, Christian-Albrechts-University of Kiel
Alexandra Blancke Soares: Bernhard-Nocht-Institute for Tropical Medicine
Tobias Spielmann: Bernhard-Nocht-Institute for Tropical Medicine
Eric Beitz: Pharmaceutical Institute, Christian-Albrechts-University of Kiel

Nature Communications, 2015, vol. 6, issue 1, 1-8

Abstract: Abstract Maintenance of a high glycolytic flow rate is critical for the rapid growth and virulence of malarial parasites. The parasites release two moles of lactic acid per mole of glucose as the anaerobic end product. However, the molecular identity of the Plasmodium lactate transporter is unknown. Here we show that a member of the microbial formate–nitrite transporter family, PfFNT, acts as a lactate/proton symporter in Plasmodium falciparum. Besides L-lactate, PfFNT transports physiologically relevant D-lactate, as well as pyruvate, acetate and formate, and is inhibited by the antiplasmodial compounds phloretin, furosemide and cinnamate derivatives, but not by p-chloromercuribenzene sulfonate (pCMBS). Our data on PfFNT monocarboxylate transport are consistent with those obtained with living parasites. Moreover, PfFNT is the only transporter of the plasmodial glycolytic pathway for which structure information is available from crystals of homologous proteins, rendering it amenable to further evaluation as a novel antimalarial drug target.

Date: 2015
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DOI: 10.1038/ncomms7284

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