Plasmodium falciparum is responsible for the most severe form of malaria and having developed resistance to current antimalarial drugs, there is a dire need to identify new targets. Blood-stage P. falciparum extensively remodels the erythrocytes it infects to help avoid host immunity and facilitate import of essential plasma nutrients to fuel rapid parasite growth. Around 500 effector proteins are synthesised by the parasite to carry out host cell modification. These effector proteins need to be exported into the erythrocyte across an enveloping parasitophorous vacuole membrane (PVM). The Plasmodium translocon of exported proteins (PTEX) is thought to span the PVM and provide a selective channel that unfolds and then extrudes proteins across the PVM into the erythrocyte. One of the major host cell modifications carried out by parasite proteins is the formation of channels at the erythrocyte membrane termed the new permeability pathways or NPPs. The NPPs provide the parasite with essential plasma nutrients and expel harmful wastes to promote parasite growth. The RhopH complex compromising RhopH1, RhopH2 and RhopH3 have recently been linked to NPP activity (Counihan et al2017, eLife). Knocking down RhopH2 resulted in reduced NPP activity and therefore we hypothesise that RhopH2 is necessary for the correct function of the NPPs. This study also showed that RhopH2 interacts with 30 exported proteins and we hypothesise that these proteins might help the RhopH complex form the NPPs. Twelve of the 30 proteins are currently being studied and by tagging the proteins and using a conditional knockdown system, we aim to confirm which exported proteins bind the RhopH complex and play a role in NPP function. Understanding how the NPPs work and what proteins are functionally involved might help target the NPPs for future therapeutic intervention.