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Cell Host Microbe. 2015 Oct 14;18(4):501-11. doi: 10.1016/j.chom.2015.09.006.

Global Analysis of Palmitoylated Proteins in Toxoplasma gondii.

Author information

1
Department of Pathology, Stanford University School of Medicine, Stanford, CA 94305, USA.
2
Department of Chemistry, University of Michigan, Ann Arbor, MI 48109, USA.
3
Department of Microbiology and Molecular Genetics, University of Vermont, Burlington, VT 05405, USA.
4
Department of Chemistry, University of Michigan, Ann Arbor, MI 48109, USA. Electronic address: brentrm@umich.edu.
5
Department of Pathology, Stanford University School of Medicine, Stanford, CA 94305, USA; Department of Microbiology and Immunology, Stanford University School of Medicine, Stanford, CA 94305, USA. Electronic address: mbogyo@stanford.edu.

Abstract

Post-translational modifications (PTMs) such as palmitoylation are critical for the lytic cycle of the protozoan parasite Toxoplasma gondii. While palmitoylation is involved in invasion, motility, and cell morphology, the proteins that utilize this PTM remain largely unknown. Using a chemical proteomic approach, we report a comprehensive analysis of palmitoylated proteins in T. gondii, identifying a total of 282 proteins, including cytosolic, membrane-associated, and transmembrane proteins. From this large set of palmitoylated targets, we validate palmitoylation of proteins involved in motility (myosin light chain 1, myosin A), cell morphology (PhIL1), and host cell invasion (apical membrane antigen 1, AMA1). Further studies reveal that blocking AMA1 palmitoylation enhances the release of AMA1 and other invasion-related proteins from apical secretory organelles, suggesting a previously unrecognized role for AMA1. These findings suggest that palmitoylation is ubiquitous throughout the T. gondii proteome and reveal insights into the biology of this important human pathogen.

PMID:
26468752
PMCID:
PMC4694575
DOI:
10.1016/j.chom.2015.09.006
[Indexed for MEDLINE]
Free PMC Article

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