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Infection by  Toxoplasma gondii  leads to massive changes to the host cell. Here, we identify a novel host cell effector export pathway that requires the Golgi-resident aspartyl protease 5 (ASP5). We demonstrate that ASP5 cleaves a highly constrained amino acid motif that has similarity to the PEXEL-motif of  Plasmodium  parasites. We show that ASP5 matures substrates at both the N- and C-terminal ends of proteins and also controls trafficking of effectors without this motif. Furthermore, ASP5 controls establishment of the nanotubular network and is required for the efficient recruitment of host mitochondria to the vacuole. Assessment of host gene expression reveals that the ASP5-dependent pathway influences thousands of the transcriptional changes that  Toxoplasma  imparts on its host cell. All these changes result in attenuation of virulence of Δ asp5  tachyzoites in vivo. This work characterizes the first identified machinery required for export of  Toxoplasma  effectors into the infected host cell.

An aspartyl protease defines a novel pathway for export of Toxoplasma proteins into the host cell