A newly discovered protein export machine in malaria parasites

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 and Brendan S. Crabb ()
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Tania F. de Koning-Ward: The Walter & Eliza Hall Institute of Medical Research
Paul R. Gilson: The Walter & Eliza Hall Institute of Medical Research
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

Nature, 2009, vol. 459, issue 7249, 945-949

Abstract: 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.

Date: 2009
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DOI: 10.1038/nature08104

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