Role of post translational modifications: glycosylation and palmitoylation in Toxoplasma gondii Public Deposited

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  • March 21, 2019
  • Luk, Flora C.
    • Affiliation: School of Medicine, Department of Cell Biology and Physiology
  • Many eukaryotic proteins are post-translationally modified to regulate protein-protein interactions, protein stability, folding, localization, and proteolysis. Modified proteins play essential roles in cellular processes such as protein-protein interactions, signal transduction, and membrane association. Given the prevalence and importance of these modifications, post translational modifications such as protein palmitoylation and glycosylation have not been explored in Toxoplasma. At the time of our study, protein glycosylation was known to modify two proteins: GAP50 and gp23. And protein palmitoylation has only been experimentally confirmed for a few parasite specific proteins although many have been predicted to have cysteine residues that are modified. This body of work explored the contributions of two key post-translational modifications, glycosylation and protein palmitoylation, to Toxoplasma biology. Toxoplasma gondii is an obligate intracellular parasite that infects more than 60 million people in the U.S. Infection can cause congenital neurological defects, and severe disease in immuno-compromised individuals. Toxoplasma survival is dependent on parasite motility, which governs essential processes: invasion, egress, and dissemination throughout the host. We described the analysis of protein glycosylation in Toxoplasma. We began with the detection of N-glycosylation of myosin XIV motor complex anchor, GAP50, and proceeded to characterize the structure and immune-reactivity of Toxoplasma N-linked glycans. Subsequently, to identify palmitoyl proteins in Toxoplasma, we took advantage of recently developed biochemical and proteomic approaches allowing us to decrease the length of time of analysis and increase the number of proteins analyzed. The palmitoyl proteome of Toxoplasma included cytoplasmic and transmembrane proteins that also had additional acylation sites. The two analysis presented below would help us identify how post-translational modifications - glycosylation and palmitoylation - regulate parasite proteins to mediate important cellular processes essential to survival.
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  • In Copyright
  • "... in partial fulfillment of the requirements for the degree of Doctor of Philosophy in the Department of Cell and Developmental Biology"
  • Beckers, Cornelis J.
Degree granting institution
  • University of North Carolina at Chapel Hill
Place of publication
  • Chapel Hill, NC
  • Open access

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