A newly discovered protein export machine in malaria parasites

作者：de Koning Ward Tania F; Gilson Paul R; Boddey Justin A; Rug Melanie; Smith Brian J; Papenfuss Anthony T; Sanders Paul R; Lundie Rachel J; Maier Alexander G; Cowman Alan F; Crabb Brendan S^*

来源：Nature, 2009, 459(7249): 945-U66.

DOI：10.1038/nature08104

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.

• 出版日期2009-6-18
• 单位迪肯大学; 河北医科大学