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; Brendan S. Crabb

doi:10.1038/nature08104

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, Brendan S. Crabb

Research output: Contribution to journal › Article › peer-review

396 Citations (Scopus)

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.

Original language	English
Pages (from-to)	945-949
Number of pages	5
Journal	Nature
Volume	459
Issue number	7249
DOIs	https://doi.org/10.1038/nature08104
Publication status	Published - 18 Jun 2009
Externally published	Yes

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@article{9d5174ab514d406fb1ac65706062247f,

title = "A newly discovered protein export machine in malaria parasites",

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.",

author = "{De Koning-Ward}, {Tania F.} and Gilson, {Paul R.} and Boddey, {Justin A.} and Melanie Rug and Smith, {Brian J.} and Papenfuss, {Anthony T.} and Sanders, {Paul R.} and Lundie, {Rachel J.} and Maier, {Alexander G.} and Cowman, {Alan F.} and Crabb, {Brendan S.}",

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T1 - A newly discovered protein export machine in malaria parasites

AU - De Koning-Ward, Tania F.

AU - Gilson, Paul R.

AU - Boddey, Justin A.

AU - Rug, Melanie

AU - Smith, Brian J.

AU - Papenfuss, Anthony T.

AU - Sanders, Paul R.

AU - Lundie, Rachel J.

AU - Maier, Alexander G.

AU - Cowman, Alan F.

AU - Crabb, Brendan S.

PY - 2009/6/18

Y1 - 2009/6/18

N2 - 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.

AB - 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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JO - Nature

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A newly discovered protein export machine in malaria parasites

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