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A newly discovered protein export machine in malaria parasites

Author

Listed:
  • Tania F. de Koning-Ward

    (The Walter & Eliza Hall Institute of Medical Research
    Deakin University, Waurn Ponds, Victoria 3217, Australia)

  • Paul R. Gilson

    (The Walter & Eliza Hall Institute of Medical Research
    Macfarlane Burnet Institute for Medical Research & Public Health)

  • Justin A. Boddey

    (The Walter & Eliza Hall Institute of Medical Research)

  • Melanie Rug

    (The Walter & Eliza Hall Institute of Medical Research)

  • Brian J. Smith

    (The Walter & Eliza Hall Institute of Medical Research)

  • Anthony T. Papenfuss

    (The Walter & Eliza Hall Institute of Medical Research)

  • Paul R. Sanders

    (The Walter & Eliza Hall Institute of Medical Research)

  • Rachel J. Lundie

    (The Walter & Eliza Hall Institute of Medical Research)

  • Alexander G. Maier

    (The Walter & Eliza Hall Institute of Medical Research)

  • Alan F. Cowman

    (The Walter & Eliza Hall Institute of Medical Research)

  • Brendan S. Crabb

    (The Walter & Eliza Hall Institute of Medical Research
    Macfarlane Burnet Institute for Medical Research & Public Health)

Abstract

Several hundred malaria parasite proteins are exported beyond an encasing vacuole and into the cytosol of the host erythrocyte, a process that is central to the virulence and viability of the causative Plasmodium species. The trafficking machinery responsible for this export is unknown. Here we identify in Plasmodium falciparum a translocon of exported proteins (PTEX), which is located in the vacuole membrane. The PTEX complex is ATP-powered, and comprises heat shock protein 101 (HSP101; a ClpA/B-like ATPase from the AAA+ superfamily, of a type commonly associated with protein translocons), a novel protein termed PTEX150 and a known parasite protein, exported protein 2 (EXP2). EXP2 is the potential channel, as it is the membrane-associated component of the core PTEX complex. Two other proteins, a new protein PTEX88 and thioredoxin 2 (TRX2), were also identified as PTEX components. As a common portal for numerous crucial processes, this translocon offers a new avenue for therapeutic intervention.

Suggested Citation

  • Tania F. de Koning-Ward & Paul R. Gilson & Justin A. Boddey & Melanie Rug & Brian J. Smith & Anthony T. Papenfuss & Paul R. Sanders & Rachel J. Lundie & Alexander G. Maier & Alan F. Cowman & Brendan S, 2009. "A newly discovered protein export machine in malaria parasites," Nature, Nature, vol. 459(7249), pages 945-949, June.
    • Handle: RePEc:nat:nature:v:459:y:2009:i:7249:d:10.1038_nature08104
    DOI: 10.1038/nature08104
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    Cited by:

    1. Madeline G. Dans & Coralie Boulet & Gabrielle M. Watson & William Nguyen & Jerzy M. Dziekan & Cindy Evelyn & Kitsanapong Reaksudsan & Somya Mehra & Zahra Razook & Niall D. Geoghegan & Michael J. Mlodz, 2024. "Aryl amino acetamides prevent Plasmodium falciparum ring development via targeting the lipid-transfer protein PfSTART1," Nature Communications, Nature, vol. 15(1), pages 1-19, December.

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