Various locations of exported Plasmodium proteins. Shown are live fluorescence micrographs of transgenic Plasmodium berghei parasites expressing mCherry-tagged versions of a Plasmodium export element reporter exported into the red blood cell (RBC) cytoplasm (part Aa), intraerythrocytic P. berghei-induced structures 1 (IBIS1) localizing to the Maurer’s cleft equivalent (part Ab) or erythrocyte membrane-associated protein 1 (EMAP1) (part Ac). Red indicates tagged protein and blue indicates the nucleus. B | Nutrient and protein traffic across the parasitophorous vacuole membrane (PVM). EXP2 (purple) forms a heptameric pore facilitating free nutrient diffusion across the PVM. The pore complex also translocates exported virulence factors (grey) on assembly with PTEX150 (yellow) and HSP101 (green). Auxiliary factors of the Plasmodium translocon of exported proteins (PTEX), including PTEX88, thioredoxin 2 and surface protein P113 (light blue), are thought to assist protein unfolding and delivery. The exported protein-interacting complex (EPIC), consisting of PV1, PV2 and the transmembrane protein EXP3 (light grey), is thought to deliver protein cargo to PTEX. On translocation, RBC chaperones, such as the TCP1 ring complex (red), might receive and refold the cargo. C | Structure of PTEX in distinct ‘engaged’ and ‘resetting’ states determined by cryo-electron microscopy (Protein Data Bank IDs 6E10 and 6E11)64. Adenosine 5′-(γ-thiotriphosphate) molecules are highlighted in red. The view from the RBC cytosol shows cargo trapped in the engaged HSP101 channel (grey, bottom). PPM, parasite plasma membrane. Matz JM, Beck JR, Blackman MJ. The parasitophorous vacuole of the blood-stage malaria parasite. Nat Rev Microbiol. 2020 18(7):379-391. PMID: 31980807.