A newly discovered protein export machine in malaria parasites
- Author(s)
- de Koning-Ward, TF; Gilson, PR; Boddey, JA; Rug, M; Smith, BJ; Papenfuss, AT; Sanders, PR; Lundie, RJ; Maier, AG; Cowman, AF; Crabb, BS;
- Details
- Publication Year 2009-06-18,Volume 459,Issue #7249,Page 945-U66
- Journal Title
- NATURE
- Publication Type
- Journal Article
- 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.
- Publisher
- NATURE PUBLISHING GROUP
- Keywords
- RED-BLOOD-CELLS; FALCIPARUM-INFECTED ERYTHROCYTES; INVASION INHIBITORY ANTIBODIES; PLASMODIUM-FALCIPARUM; HOST ERYTHROCYTE; TARGETING SIGNAL; BINDING PROTEIN; TRAFFICKING; VIRULENCE; SURFACE
- Publisher's Version
- https://doi.org/10.1038/nature08104
- Terms of Use/Rights Notice
- Refer to copyright notice on published article.
Creation Date: 2009-06-18 12:00:00