Apicomplexan parasites cause major human disease and food insecurity. They owe their considerable success to highly specialized cell compartments and structures. These adaptations drive their recognition, nondestructive penetration, and elaborate reengineering of the host's cells to promote their growth, dissemination, and the countering of host defenses. The evolution of unique apicomplexan cellular compartments is concomitant with vast proteomic novelty. Consequently, half of apicomplexan proteins are unique and uncharacterized. Here, we determine the steady-state subcellular location of thousands of proteins simultaneously within the globally prevalent apicomplexan parasite Toxoplasma gondii. This provides unprecedented comprehensive molecular definition of these unicellular eukaryotes and their specialized compartments, and these data reveal the spatial organizations of protein expression and function, adaptation to hosts, and the underlying evolutionary trajectories of these pathogens.
KAUST Repository Item: Exported on 2020-10-19
Acknowledged KAUST grant number(s): BAS/1/1020-01-01, OSR-2015-CRG4-2610
Acknowledgements: This work was supported by the Medical Research Council, United Kingdom, MR/M011690/1 to R.F.W.; King Abdullah University of Science and Technology (KAUST), Saudi Arabia, OSR-2015-CRG4-2610 to A.P., R.F.W., and K.S.L.; Wellcome Trust, United Kingdom, Investigator award 214298/Z/18/Z to R.F.W.; an Isaac Newton Trust-Leverhulme, Early Career Fellowship ECF-2015-562 to K.B; and KAUST faculty baseline funding (BAS/1/1020-01-01) to A.P. Mass spectrometry data were acquired by Mike Deery at the Cambridge Centre of Proteomics, and we thank Laurent Gatto for useful discussions.