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. Author manuscript; available in PMC: 2019 Jun 24.
Published in final edited form as: Methods Mol Biol. 2019;1955:287–308. doi: 10.1007/978-1-4939-9148-8_22

Fig 1.

Fig 1.

Schematic representation of T. cruzi trypomastigote surface coat. (Left panels) T. cruzi contains a complex cell surface consisting of several glycoconjugates inserted into the plasma membrane via a GPI anchor. These glycoconjugates include GIPL and GPI-anchored proteins (GPI-APs) (tGPI-mucin, TS, and MASP). (Middle panel) tGPI-mucin contains a protein core heavily glycosylated with O-glycans linked to threonine (Thr) (rarely to serine) residues via an α-N-acetylglucosamine (α-GlcNAc). (Right panel) tGPI-mucin specifically contains terminal, nonreducing α-galactopyranose (α-Galp) residues, which serve as the major targets for the highly abundant, lytic anti-α-Gal Abs, produced during both the acute and chronic phases of ChD. A small portion of these O-glycans (10%) exist as linear trisaccharides (Galα1,3Galβ1,4GlcNAcα), while the remaining 90% of the structures are branched and are as-yet to be structurally characterized. The hypothetical linkages (*) of the branched O-glycans are based on partial liquid chromatography-tandem mass spectrometry (LC-MS/MS) data analysis, following beta-elimination and permethylation of tGPI-mucin-derived O-glycans (Almeida et al., unpublished data).