A Comprehensive Subcellular Atlas of the Toxoplasma Proteome via hyperLOPIT Provides Spatial Context for Protein Functions.
Type
ArticleAuthors
Barylyuk, KonstantinKoreny, Ludek
Ke, Huiling
Butterworth, Simon
Crook, Oliver M
Lassadi, Imen
Gupta, Vipul
Tromer, Eelco
Mourier, Tobias
Stevens, Tim J
Breckels, Lisa M
Pain, Arnab

Lilley, Kathryn S
Waller, Ross F
KAUST Department
Biological and Environmental Sciences and Engineering (BESE) DivisionBioscience Program
Pathogen Genomics Laboratory
KAUST Grant Number
BAS/1/1020-01-01OSR-2015-CRG4-2610
Date
2020-10-13Online Publication Date
2020-10-13Print Publication Date
2020-11Submitted Date
2020-05-11Permanent link to this record
http://hdl.handle.net/10754/665619
Metadata
Show full item recordAbstract
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.Citation
Barylyuk, K., Koreny, L., Ke, H., Butterworth, S., Crook, O. M., Lassadi, I., … Waller, R. F. (2020). A Comprehensive Subcellular Atlas of the Toxoplasma Proteome via hyperLOPIT Provides Spatial Context for Protein Functions. Cell Host & Microbe. doi:10.1016/j.chom.2020.09.011Sponsors
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.Publisher
Elsevier BVJournal
Cell host & microbePubMed ID
33053376Additional Links
https://linkinghub.elsevier.com/retrieve/pii/S193131282030514Xae974a485f413a2113503eed53cd6c53
10.1016/j.chom.2020.09.011
Scopus Count
Except where otherwise noted, this item's license is described as This is an open access article under the CC BY license.
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