Plasmodium parasites that cause malaria spend part of their life cycle within human host hepatocytes and red blood cells (RBCs) where they extensively remodel the infected cells through the export of hundreds of parasite proteins. These proteins play many roles including altering the infected RBC (iRBC) membrane permeability to acquire nutrients required for survival, increased pathogenesis and host immune evasion. Proteins are secreted from the parasite into the parasitophorous vacuole, surrounding the parasite within the infected cell. They must then pass across the parasitophorous vacuole membrane (PVM) into the RBC cytoplasm. It has previously been shown that a protein complex, the Plasmodium Translocon of EXported proteins (PTEX), is found on the PVM and is most likely the protein translocating channel or translocon responsible for this export process1 . Here we show that we are able to inducibly knock-down the levels of PTEX150, a core component of the translocon, within parasites. Even a relatively low level of protein knockdown leads to a significant decrease in the ability of the parasite to grow, eventually leading to death. This demonstrates the importance of this complex to the malaria parasite and validates it as a viable drug target. We are currently investigating the ability of these PTEX knockdown parasite lines to export proteins into the host RBC to validate its role as a translocon using a number of techniques, including the use exported luciferase reporter proteins.