This chapter describes the range of glycan structures and pathways that are found in different parasitic protozoa. All parasitic protists express a range of glycoconjugates that form protective protein-rich or carbohydrate-rich surface coats. Protein-rich coats are typically found on developmental stages that inhabit nonhydrolytic niches, such as the bloodstream and nonacidified intracellular vacuoles. These coats are commonly dominated by a limited repertoire of antigenically diverse proteins that are commonly, but not always, glycosylphosphatidylinositol- (GPI-) anchored and modified with N- or O-glycans. Carbohydrate-rich coats are commonly found on developmental stages that dwell within hydrolytic environments, such as vertebrate and arthropod digestive tracts and lysosomal vacuoles. These coats are dominated by GPI-anchored glycoproteins that are heavily modified with N-glycans, O-glycans, or phosphoglycans. Free GPI glycolipids (not attached to protein) can also be abundant or dominant components of these coats. Some parasitic protists can also form highly resistant cyst stages encased within polysaccharide-rich cell walls. Considerable progress has been made in defining the structures of the surface and intracellular glycans of the parasitic protists, their biosynthesis and the role that individual components play in parasite infectivity.
O-glycosylation, Glycosylphosphatidylinositol, N-glycosylation, protozoan parasites, Phosphoglycosylation
Publication DOI: 10.1016/B978-0-12-374546-0.00012-2Publisher: Amsterdam: Elsevier
Correspondence: malcolmm@unimelb.edu.au
Editors: Moran A
Institutions: Department of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, Australia
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