Plasmodium Translocon of Exported Proteins (PTEX)

The Plasmodium Translocon of Exported Proteins (PTEX) is a multi-protein machinery located at the parasitophorous vacuole membrane (PVM) of the malaria parasite Plasmodium falciparum (Elsworth et al., 2014, Nature). It is responsible for the export of hundreds of parasite proteins into the host red blood cell, a process that is fundamental for the parasite's survival, nutrient uptake, and pathogenesis (Beck et al., 2014, Nature). The complex consists of five core components: the AAA+ ATPase HSP101, PTEX150, the pore-forming EXP2, PTEX88, and TRX2 (Ho et al., 2018, Nature). PTEX facilitates the translocation of virulence factors, such as the PfEMP1 adhesin, which allows the parasite to remodel the host cell and evade the immune system (de Koning-Ward et al., 2015, Annual Review of Microbiology). Given its essential role in the asexual blood stage and its lack of a direct human homolog, PTEX is a high-priority target for the development of next-generation antimalarials (Matthews et al., 2019, Protein Science). Experimental inhibitors like WEHI-842 and the drug ivermectin have demonstrated the potential to disrupt this transport system, effectively arresting parasite development (Nyboer et al., 2018, Journal of Biological Chemistry).

Other names

PTEX complexPlasmodium protein export machineryPVM transloconPlasmodium falciparum protein transport system

Inhibition of the ATP-dependent translocation of parasite-encoded effector proteins across the parasitophorous vacuole membrane into the host erythrocyte.