A newly discovered protein export machine in malaria parasites

被引:365
作者
de Koning-Ward, Tania F. [1 ,2 ]
Gilson, Paul R. [1 ,3 ]
Boddey, Justin A. [1 ]
Rug, Melanie [1 ]
Smith, Brian J. [1 ]
Papenfuss, Anthony T. [1 ]
Sanders, Paul R. [1 ]
Lundie, Rachel J. [1 ]
Maier, Alexander G. [1 ]
Cowman, Alan F. [1 ]
Crabb, Brendan S. [1 ,3 ]
机构
[1] Walter & Eliza Hall Inst Med Res, Melbourne, Vic 3052, Australia
[2] Deakin Univ, Waurn Ponds, Vic 3217, Australia
[3] Macfarlane Burnet Inst Med Res & Publ Hlth, Melbourne, Vic 3004, Australia
基金
澳大利亚国家健康与医学研究理事会;
关键词
PLASMODIUM-FALCIPARUM; TARGETING SIGNAL; BINDING PROTEIN; VIRULENCE; SURFACE; TRAFFICKING; COMPLEXES; INVASION; ANTIGEN; CYTOADHERENCE;
D O I
10.1038/nature08104
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
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.
引用
收藏
页码:945 / U66
页数:6
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