A subcellular atlas of Toxoplasma reveals the functional context of the proteome
Crook, Oliver M
Tromer, Eelco C
Stevens, Tim J
Breckels, Lisa M
Lilley, Kathryn S
Waller, Ross F
KAUST DepartmentBiological and Environmental Sciences and Engineering (BESE) Division
Pathogen Genomics Laboratory
Permanent link to this recordhttp://hdl.handle.net/10754/662636
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AbstractApicomplexan parasites cause major human disease and food insecurity. They owe their considerable success to novel, highly specialized cell compartments and structures. These adaptations drive their recognition and non-destructive penetration of host′s cells and the elaborate reengineering of these cells to promote growth, dissemination, and the countering of host defenses. The evolution of unique apicomplexan cellular compartments is concomitant with vast proteomic novelty that defines these new cell organizations and their functions. Consequently, half of apicomplexan proteins are unique and uncharacterized, and these cells are, therefore, very poorly understood. 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 to these cells and their novel compartments, and these data reveal the spatial organizations of protein expression and function, adaptation to hosts, and the underlying evolutionary trajectories of these pathogens.
CitationBarylyuk, K., Koreny, L., Ke, H., Butterworth, S., Crook, O. M., Lassadi, I., … Waller, R. F. (2020). A subcellular atlas of Toxoplasma reveals the functional context of the proteome. doi:10.1101/2020.04.23.057125
SponsorsWe thank John Boothroyd, Peter Bradley, Mark Carrington, Vern Carruthers, Maryse Lebrun, Corinne Mercier, David Sibley, Dominque Soldati-Favre, Boris Striepen, Giel van Dooren and Gary Ward for generous gifts of antibodies used in this study. Mass spectrometry data were acquired by Mike Deery at the Cambridge Centre of Proteomics, and we thank Laurent Gatto for useful discussions. This work was supported by the Medical Research Council MR/M011690/1 to R.F.W., King Abdullah University of Science and Technology (KAUST) OSR-2015-CRG4-2610 to A.P., R.F.W. and K.S.L., Wellcome Trust Investigator Award 214298/Z/18/Z to R.F.W, a 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.
PublisherCold Spring Harbor Laboratory