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Plasmepsin V shows its carnivorous side

Nature Structural & Molecular Biology volume 22, pages 647–648 (2015)Cite this article

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An Erratum to this article was published on 04 November 2015

This article has been updated

Export of effector proteins is crucial for the virulence program of the malaria parasite Plasmodium falciparum. A crystal structure of the Plasmodium vivax processing enzyme essential for protein export reveals noncanonical aspartic protease features and provides an avenue for antimalarial drug development.

To win the host-parasite battle, intraerythrocytic P. falciparum synthesizes and exports hundreds of proteins that transmogrify the host erythrocyte1,2. Some generate various vesicular structures, membranous cisternae called Maurer's clefts, and submembrane knobs, whose functions collectively include protein trafficking, sorting and surface presentation of a variant endothelial adhesin called PfEMP1. Other exported proteins modify or rigidify the erythrocyte cytoskeleton. Still others establish new permeation pathways by which parasites gain access to bloodstream nutrients. Some exported proteins facilitate intracellular communication. Yet others may have systemic roles in the host.

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Figure 1: Features of plasmepsin V.

Katie Vicari/Nature Publishing Group

Change history

  • 12 October 2015

    In the version of this article initially published, the strapline mistakenly described a crystal structure of the Plasmodium falciparum enzyme. Plasmodium vivax is the correct species. The error has been corrected in the HTML and PDF versions of the article.

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  1. Daniel E. Goldberg is at the Department of Medicine and Department of Molecular Microbiology, Washington University School of Medicine, St. Louis, Missouri, USA.

    Daniel E Goldberg

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Correspondence to Daniel E Goldberg.

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Goldberg, D. Plasmepsin V shows its carnivorous side. Nat Struct Mol Biol 22, 647–648 (2015). https://doi.org/10.1038/nsmb.3077

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