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A Comprehensive Subcellular Atlas of the Toxoplasma Proteome via hyperLOPIT Provides Spatial Context for Protein Functions.
Barylyuk, Konstantin; Koreny, 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.
Affiliation
  • Barylyuk K; Department of Biochemistry, University of Cambridge, Cambridge CB2 1QW, UK. Electronic address: kb601@cam.ac.uk.
  • Koreny L; Department of Biochemistry, University of Cambridge, Cambridge CB2 1QW, UK.
  • Ke H; Department of Biochemistry, University of Cambridge, Cambridge CB2 1QW, UK.
  • Butterworth S; Department of Biochemistry, University of Cambridge, Cambridge CB2 1QW, UK.
  • Crook OM; Department of Biochemistry, University of Cambridge, Cambridge CB2 1QW, UK; Milner Therapeutics Institute, Jeffrey Cheah Biomedical Centre, University of Cambridge, Cambridge CB20 0AW, UK; MRC Biostatistics Unit, Cambridge Institute for Public Health, Cambridge CB2 0SR, UK.
  • Lassadi I; Department of Biochemistry, University of Cambridge, Cambridge CB2 1QW, UK.
  • Gupta V; Department of Biochemistry, University of Cambridge, Cambridge CB2 1QW, UK.
  • Tromer E; Department of Biochemistry, University of Cambridge, Cambridge CB2 1QW, UK.
  • Mourier T; Biological and Environmental Science and Engineering Division, King Abdullah University of Science and Technology, Thuwal 23955, Saudi Arabia.
  • Stevens TJ; MRC Laboratory of Molecular Biology, Cambridge CB2 0QH, UK.
  • Breckels LM; Department of Biochemistry, University of Cambridge, Cambridge CB2 1QW, UK; Milner Therapeutics Institute, Jeffrey Cheah Biomedical Centre, University of Cambridge, Cambridge CB20 0AW, UK.
  • Pain A; Biological and Environmental Science and Engineering Division, King Abdullah University of Science and Technology, Thuwal 23955, Saudi Arabia; Global Station for Zoonosis Control, Gi-CoRE, Hokkaido University, Sapporo 060-0808, Japan; Nuffield Division of Clinical Laboratory Sciences (NDCLS), Univer
  • Lilley KS; Department of Biochemistry, University of Cambridge, Cambridge CB2 1QW, UK; Milner Therapeutics Institute, Jeffrey Cheah Biomedical Centre, University of Cambridge, Cambridge CB20 0AW, UK.
  • Waller RF; Department of Biochemistry, University of Cambridge, Cambridge CB2 1QW, UK. Electronic address: rfw26@cam.ac.uk.
Cell Host Microbe ; 28(5): 752-766.e9, 2020 11 11.
Article in En | MEDLINE | ID: mdl-33053376
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.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Toxoplasma / Protozoan Proteins / Proteome Limits: Humans Language: En Journal: Cell Host Microbe Journal subject: MICROBIOLOGIA Year: 2020 Document type: Article

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Toxoplasma / Protozoan Proteins / Proteome Limits: Humans Language: En Journal: Cell Host Microbe Journal subject: MICROBIOLOGIA Year: 2020 Document type: Article