A newly discovered protein export machine in malaria parasites

Nature. 2009 Jun 18;459(7249):945-9. doi: 10.1038/nature08104.

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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Animals, Genetically Modified
  • Malaria, Falciparum / parasitology*
  • Models, Biological
  • Multiprotein Complexes / chemistry*
  • Multiprotein Complexes / metabolism*
  • Plasmodium falciparum / metabolism*
  • Protein Binding
  • Protein Transport
  • Protozoan Proteins / metabolism*

Substances

  • Multiprotein Complexes
  • Protozoan Proteins