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Plasmepsin V licenses Plasmodium proteins for export into the host erythrocyte

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  • Ilaria Russo

    (Howard Hughes Medical Institute, Washington University School of Medicine, St Louis, Missouri 63110, USA
    Present address: Department of Experimental Medicine and Biochemical Science, University of Perugia, 06126 Perugia, Italy.)

  • Shalon Babbitt

    (Howard Hughes Medical Institute, Washington University School of Medicine, St Louis, Missouri 63110, USA)

  • Vasant Muralidharan

    (Howard Hughes Medical Institute, Washington University School of Medicine, St Louis, Missouri 63110, USA)

  • Tamira Butler

    (Howard Hughes Medical Institute, Washington University School of Medicine, St Louis, Missouri 63110, USA)

  • Anna Oksman

    (Howard Hughes Medical Institute, Washington University School of Medicine, St Louis, Missouri 63110, USA)

  • Daniel E. Goldberg

    (Howard Hughes Medical Institute, Washington University School of Medicine, St Louis, Missouri 63110, USA)

Abstract

During their intraerythrocytic development, malaria parasites export hundreds of proteins to remodel their host cell. Nutrient acquisition, cytoadherence and antigenic variation are among the key virulence functions effected by this erythrocyte takeover. Proteins destined for export are synthesized in the endoplasmic reticulum (ER) and cleaved at a conserved (PEXEL) motif, which allows translocation into the host cell via an ATP-driven translocon called the PTEX complex. We report that plasmepsin V, an ER aspartic protease with distant homology to the mammalian processing enzyme BACE, recognizes the PEXEL motif and cleaves it at the correct site. This enzyme is essential for parasite viability and ER residence is essential for its function. We propose that plasmepsin V is the PEXEL protease and is an attractive enzyme for antimalarial drug development.

Suggested Citation

  • Ilaria Russo & Shalon Babbitt & Vasant Muralidharan & Tamira Butler & Anna Oksman & Daniel E. Goldberg, 2010. "Plasmepsin V licenses Plasmodium proteins for export into the host erythrocyte," Nature, Nature, vol. 463(7281), pages 632-636, February.
    • Handle: RePEc:nat:nature:v:463:y:2010:i:7281:d:10.1038_nature08726
    DOI: 10.1038/nature08726
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