A newly discovered protein export machine in malaria parasites.
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.
de Koning-Ward
Tania F
TF
The Walter & Eliza Hall Institute of Medical Research, Melbourne 3052, Australia.
Gilson
Paul R
PR
Boddey
Justin A
JA
Rug
Melanie
M
Smith
Brian J
BJ
Papenfuss
Anthony T
AT
Sanders
Paul R
PR
Lundie
Rachel J
RJ
Maier
Alexander G
AG
Cowman
Alan F
AF
Crabb
Brendan S
BS
D000818:Animals; D030801:Animals, Genetically Modified; D016778:Malaria, Falciparum / Q000469:parasitology*; D008954:Models, Biological; D046912:Multiprotein Complexes / Q000737:chemistry* / Q000378:metabolism*; D010963:Plasmodium falciparum / Q000378:metabolism*; D011485:Protein Binding; D021381:Protein Transport; D015800:Protozoan Proteins / Q000378:metabolism*
D046912:Multiprotein Complexes; D015800:Protozoan Proteins