Authors

Discussion

Protein glycosylation is one of the most abundant and widespread post-translational modifications (PTMs). This PTM class is involved in many biological processes including host-pathogen interactions and protein quality control and therefore plays a role in many key aspects of parasite biology.

Toxoplasma gondii is an opportunistic pathogen of humans that is estimated to infect up to 30% of the world population. Different glycosylation pathways have been shown to affect the kinetics of protein folding and stabilisation in the parasite. O-fucosylation of nucleocytoplasmic proteins by TgSPY, a paralog of host O-GlcNAc transferase (OGT), is one of these pathways. This modification affects protein steady state levels, resulting in slower parasite replication and differentiation to the chronic stage in vitro. 

Additionally, complementation of spy-deficient parasites with specifically selected mutants allows the study of the biochemistry and evolution of this family of glycosyltransferases in a cell system, highlighting the importance of divergent protozoa as model organisms.