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Protein structure reveals how a malaria parasite imports a wide range of sugars

Unlike many sugar-transporting proteins, a transporter in one species of malaria parasite can import several types of sugar equally effectively, aiding the parasite’s survival. The structure of this protein reveals the reason for its versatility.
  1. Thorsten Althoff

    1. Thorsten Althoff is in the Department of Physiology, University of California, Los Angeles, Los Angeles, California 90095, USA.

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  2. Jeff Abramson

    1. Jeff Abramson are in the Department of Physiology, University of California, Los Angeles, Los Angeles, California 90095, USA.

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Most cases of malaria are caused by the protozoan parasite Plasmodium falciparum1. Given that there are more than 400,000 malaria-associated deaths annually, and that P. falciparum is constantly evolving to resist pharmacological therapies, opportunities for developing drugs that target this organism must be continuously explored. A protein called the P. falciparum hexose transporter 1 (PfHT1) has a proclivity for scavenging sugars from an infected host’s red blood cells to improve the parasite’s chances of survival in these cells, and is therefore a drug target. Writing in Nature, Qureshi et al.2 describe the 3D structure of PfHT1, and identify a mechanism that couples the docking of a sugar in the PfHT1 binding site to the process by which sugars are gated through the protein. This coupling facilitates the protein’s substrate promiscuity — that is, its ability to transport a wide range of sugar molecules effectively, a feature that gives the parasite a distinct survival advantage.

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Nature 578, 220-221 (2020)

doi: https://doi.org/10.1038/d41586-020-00148-8

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