Journal
BIOCHEMISTRY
Volume 43, Issue 37, Pages 11889-11897Publisher
AMER CHEMICAL SOC
DOI: 10.1021/bi048942u
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Sialoglycoprotein from Trypanosoma cruzi strains participates in important biological functions in which the O-linked glycans play a pivotal role, and their structural diversity may be related to the parasite's virulence pattern. To provide supporting evidence for this idea, we have determined the structure of novel linear and branched alpha-O-GlcNAc-linked oligosaccharides present on the mucins of the T. cruzi Tulahuen strain. The O-lycans were isolated as oligosaccharide alditols by reductive beta-elimination, purified, and characterized by nuclear magnetic resonance spectroscopy and methylation analysis. Two core families were synthesized by the parasite: the Galfbeta1-->4GlcNAc and Galpbeta1-->4GlcNAc. The Galfbeta1-->4GlcNAc core yields three series of O-chain structures. In the first, the Galf residue is nonsubstituted, while in the other series it is elongated by the activity of galactopyranosyl or galactofuranosyl transferases giving rise to Galp-beta-(1-->2)-Galf-beta-(1-->4) or Gaf-beta-(1-->2)-Galf-beta-(1-->4) substructures not previously observed. The three series can arise by further galactopyranosylation of the GlcNAc O-6 arm. Sialylation was the only observed elaboration of the Galpbeta1-->4GlcNAc core family. Thus the determination of the structures of the O-glycans from T. cruzi Tulahuen mucins confirms the strain specificity of the glycosylation and predicts a relationship between it and parasite pathogenicity and the epidemiology of Chagas' disease.
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