Article

Nature 459, 945-949 (18 June 2009) | doi:10.1038/nature08104; Received 11 April 2009; Accepted 30 April 2009

A newly discovered protein export machine in malaria parasites

Tania F. de Koning-Ward1,2, Paul R. Gilson1,3, Justin A. Boddey1, Melanie Rug1, Brian J. Smith1, Anthony T. Papenfuss1, Paul R. Sanders1, Rachel J. Lundie1, Alexander G. Maier1, Alan F. Cowman1 & Brendan S. Crabb1,3

  1. The Walter & Eliza Hall Institute of Medical Research, Melbourne 3052, Australia
  2. Deakin University, Waurn Ponds, Victoria 3217, Australia
  3. Macfarlane Burnet Institute for Medical Research & Public Health, Melbourne 3004, Australia

Correspondence to: Brendan S. Crabb1,3 Correspondence and requests for materials should be addressed to B.S.C. (Email: crabb@burnet.edu.au).

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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.

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