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 Gerd Maier, Alan Frederick Cowman, Brendan S. Crabb

Research output: Contribution to journalArticleResearchpeer-review

303 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)945-949
Number of pages5
Issue number7249
Publication statusPublished - 18 Jun 2009
Externally publishedYes

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