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 β-galactofuranose (β-Galf) residue
attached to an α-N-acetylglucosamine (α-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 β-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.
