A Comprehensive Subcellular Atlas of the Toxoplasma Proteome via hyperLOPIT Provides Spatial Context for Protein Functions.

Konstantin Barylyuk; Ludek Koreny; Huiling Ke; Simon Butterworth; Oliver M Crook; Imen Lassadi; Vipul Gupta; Eelco Tromer; Tobias Mourier; Tim J Stevens; Lisa M Breckels; Arnab Pain; Kathryn S Lilley; Ross F Waller

doi:10.1016/j.chom.2020.09.011

A Comprehensive Subcellular Atlas of the Toxoplasma Proteome via hyperLOPIT Provides Spatial Context for Protein Functions.

Konstantin Barylyuk, Ludek Koreny, Huiling Ke, Simon Butterworth, Oliver M Crook, Imen Lassadi, Vipul Gupta, Eelco Tromer, Tobias Mourier, Tim J Stevens, Lisa M Breckels, Arnab Pain, Kathryn S Lilley, Ross F Waller

Research output: Contribution to journal › Article › peer-review

181 Scopus citations

Abstract

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.

Original language	English (US)
Journal	Cell Host & Microbe
DOIs	https://doi.org/10.1016/j.chom.2020.09.011
State	Published - Oct 14 2020

Bibliographical note

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.

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1016/j.chom.2020.09.011

https://repository.kaust.edu.sa/bitstream/10754/665619/1/A%20comprehensive.pdf

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Barylyuk, K., Koreny, L., Ke, H., Butterworth, S., Crook, O. M., Lassadi, I., Gupta, V., Tromer, E., Mourier, T., Stevens, T. J., Breckels, L. M., Pain, A., Lilley, K. S., & Waller, R. F. (2020). A Comprehensive Subcellular Atlas of the Toxoplasma Proteome via hyperLOPIT Provides Spatial Context for Protein Functions. Cell Host & Microbe. https://doi.org/10.1016/j.chom.2020.09.011

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title = "A Comprehensive Subcellular Atlas of the Toxoplasma Proteome via hyperLOPIT Provides Spatial Context for Protein Functions.",

abstract = "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.",

author = "Konstantin Barylyuk and Ludek Koreny and Huiling Ke and Simon Butterworth and Crook, {Oliver M} and Imen Lassadi and Vipul Gupta and Eelco Tromer and Tobias Mourier and Stevens, {Tim J} and Breckels, {Lisa M} and Arnab Pain and Lilley, {Kathryn S} and Waller, {Ross F}",

note = "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.",

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AU - Butterworth, Simon

AU - Crook, Oliver M

AU - Lassadi, Imen

AU - Gupta, Vipul

AU - Tromer, Eelco

AU - Mourier, Tobias

AU - Stevens, Tim J

AU - Breckels, Lisa M

AU - Pain, Arnab

AU - Lilley, Kathryn S

AU - Waller, Ross F

N1 - 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.

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AB - 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.

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ER -

A Comprehensive Subcellular Atlas of the Toxoplasma Proteome via hyperLOPIT Provides Spatial Context for Protein Functions.

Abstract

Bibliographical note

UN SDGs

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