The malaria PTEX component PTEX 88 interacts most closely with HSP 101 at the host–parasite interface

The pathogenic nature of malaria infections is due in part to the export of hundreds of effector proteins that actively remodel the host erythrocyte. The Plasmodium translocon of exported proteins ( PTEX ) has been shown to facilitate the trafficking of proteins into the host cell, a process that is essential for the survival of the parasite. The role of the auxiliary PTEX component PTEX 88 remains unclear, as previous attempts to elucidate its function through reverse genetic approaches showed that in contrast to the core components PTEX 150 and HSP 101, knockdown of PTEX 88 did not give rise to an export phenotype. Here, we have used biochemical approaches to understand how PTEX 88 assembles within the translocation machinery. Proteomic analysis of the PTEX 88 interactome showed that PTEX 88 interacts closely with HSP 101 but has a weaker affinity with the other core constituents of PTEX . PTEX 88 was also found to associate with other PV ‐resident proteins, including chaperones and members of the exported protein‐interacting complex that interacts with the major virulence factor Pf EMP 1, the latter contributing to cytoadherence and parasite virulence. Despite being expressed for the duration of the blood‐stage life cycle, PTEX 88 was only discretely observed at the parasitophorous vacuole membrane during ring stages and could not always be detected in the major high molecular weight complex that contains the other core components of PTEX , suggesting that its interaction with the PTEX complex may be dynamic. Together, these data have enabled the generation of an updated model of PTEX that now includes how PTEX 88 assembles within the complex.