Taxonomic group: protista / Evosea (Phylum: Evosea)
Organ / tissue: Life stage: trophozoite
Associated disease: intestinal infections due to Entamoeba [ICD11: 1A36.0 , ICD11: XN3S1 ]; amoebic liver abscess [ICD11: 1A36.10 , ICD11: XN3S1 ]; infection due to Entamoeba histolytica [ICD11: XN82F ]
 
Publication DOI: 10.1016/B978-0-12-374546-0.00012-2
Publisher: Amsterdam: Elsevier
Editors: Moran A
Correspondence: malcolmmunimelb.edu.au
Institutions: Department of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, Australia

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

Structure type: structural motif or average structure
Location inside paper: p. 207, Fig. 12.2, p.212
Compound class: GPI-anchor
Contained glycoepitopes: IEDB_115013,IEDB_120354,IEDB_123890,IEDB_130645,IEDB_130701,IEDB_131186,IEDB_134624,IEDB_135818,IEDB_136906,IEDB_137472,IEDB_141181,IEDB_141793,IEDB_141794,IEDB_141807,IEDB_144983,IEDB_144987,IEDB_151528,IEDB_151531,IEDB_152206,IEDB_153220,IEDB_190606,IEDB_742246,IEDB_918313,IEDB_983930,SB_163,SB_198,SB_31,SB_44,SB_67,SB_7,SB_72,SB_87
 
Comments, role: review; LIP = C30:1; The GPI anchor of the E. histolytica PPG contains a divergent Gal1Man2GlcN-backbone. The site of side chain attachment to this backbone is unknown.
 
NCBI Taxonomy refs (TaxIDs): 5759
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