4.2 Article Proceedings Paper

α-N-acetylglucosamine-linked O-glycans of sialoglycoproteins (Tc-mucins) from Trypanosoma cruzi Colombiana strain

Journal

MEMORIAS DO INSTITUTO OSWALDO CRUZ
Volume 104, Issue -, Pages 270-274

Publisher

FUNDACO OSWALDO CRUZ
DOI: 10.1590/S0074-02762009000900035

Keywords

Trypanosoma cruzi; NMR spectroscopy; glycoconjugate; Colombiana strain; mucins; sialic acid

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Trypanosoma cruzi sialoglycoproteins (Tc-mucins) are mucin-like molecules linked to a parasite membrane via a glycosylphosphatidylinositol anchor. We previously determined the structures of Tc-mucin O-glycan domains from several T. cruzi strains and observed significant differences among them. We now report the amino acid content and structure of Tc-mucin O-glycan chains from T. cruzi Colombiana, a strain resistant to common trypanocidal drugs. Amino acid analysis demonstrated the predominance of threonine residues (42%) and helped to identify the O-glycans as belonging to a Tc-mucin family that contain a beta-galactofuranose (beta-Galf) residue attached to an alpha-N-acetylglucosamine (alpha-GlcNAc) O-4, with the most complex glycan, a pentasaccharide-GlcNAc-ol with a branched trigalactopyranose chain, on the GlcNAc O-6. The presence of beta-Galf on O-glycans from T. cruzi Colombiana mucins supports the use of glycosylation as a phylogenetic marker for the classification of Colombiana in the T. cruzi I group.

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