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    A subcellular atlas of Toxoplasma reveals the functional context of the proteome

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    Type
    Preprint
    Authors
    Barylyuk, Konstantin cc
    Koreny, Ludek cc
    Ke, Huiling cc
    Butterworth, Simon cc
    Crook, Oliver M cc
    Lassadi, Imen cc
    Gupta, Vipul cc
    Tromer, Eelco C cc
    Mourier, Tobias
    Stevens, Tim J cc
    Breckels, Lisa M
    Pain, Arnab cc
    Lilley, Kathryn S cc
    Waller, Ross F cc
    KAUST Department
    Biological and Environmental Sciences and Engineering (BESE) Division
    Bioscience Program
    Pathogen Genomics Laboratory
    KAUST Grant Number
    BAS/1/1020-01-01
    OSR-2015-CRG4-2610
    Date
    2020-04-23
    Permanent link to this record
    http://hdl.handle.net/10754/662636
    
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    Abstract
    Apicomplexan 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.
    Citation
    Barylyuk, 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
    Sponsors
    We 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.
    Publisher
    Cold Spring Harbor Laboratory
    DOI
    10.1101/2020.04.23.057125
    Additional Links
    http://biorxiv.org/lookup/doi/10.1101/2020.04.23.057125
    https://www.biorxiv.org/content/biorxiv/early/2020/04/23/2020.04.23.057125.full.pdf
    ae974a485f413a2113503eed53cd6c53
    10.1101/2020.04.23.057125
    Scopus Count
    Collections
    Biological and Environmental Science and Engineering (BESE) Division; Preprints; Bioscience Program

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