Core α1→3‐fucose is a common modification of N‐glycans in parasitic helminths and constitutes an important epitope for IgE from Haemonchus contortus infected sheep

Abstract

Synthesis of parasite specific IgE plays a critical role in the defence against helminth infections. We report here that IgE from serum from Schistosoma mansoni infected mice and Haemonchus contortus infected sheep recognizes complex-type N-glycans from Arabidopsis thaliana, which contain R-L1C C2-Xyl) modifications, and honeybee phospholipase A2, which carries Nglycans that contain the core K K1C C3-Fuc epitope. Evidence is presented that core K K1C C3-fucosylated N-glycans bind a substantial part of the parasite specific IgE in serum of H. contortus infected sheep. These results suggest that the core K K1C C3-Fuc antigen may contribute to induction of a Th2 response leading to the production of IgE. In addition we show here that N-glycans carrying core K K1C C3-Fuc and L L1C C2-Xyl antigens are synthesized by many parasitic helminths and also by the free living nematode Caenorhabditis elegans. Since Nglycans containing the core K K1C C3-Fuc have also been implicated in honeybee and plant induced allergies, this conserved glycan might represent an important common IgE epitope.z 1999 Federation of European Biochemical Societies.

Molecular Basis of Anti-horseradish Peroxidase Staining in Caenorhabditis elegans

“…Whereas anti-HRP is a polyclonal antibody shown previously to bind both core ␣1,3-fucose and ␤1,2-xylose (11, 34 -36), anti-bee venom antisera contain a proportion of antibodies recognizing core ␣1,3-fucose on insect and plant glycoproteins (37), and the monoclonal antibody YZ1/2.23 has been shown to bind core ␣1,3-fucose (11,34,38). In the present study, previous Western blotting results (39) were confirmed that showed that anti-horseradish peroxidase binds wild-type C. elegans glycoproteins; furthermore, anti-bee venom and YZ1/2.23 also showed cross-reactivity (Fig. 1A).…”

“…In C. elegans, expression of this epitope appears to be restricted to 10% of the neurons (12), and indeed fut-1 is apparently only expressed in specific neural cells (16). However, from the viewpoint of the wider importance of nematodes as parasites, more significant is that core ␣1,3-fucose is a known IgE epitope (39,57), and so the presence of this epitope on excretory-secretory antigens, for example (as shown previously by antibody binding for H. contortus (39)), may have a role in the interactions of parasitic nematodes with their hosts. C. elegans also shares carbohydrate epitopes with H. contortus that induce protective immunity (58).…”

Comprehensive Analysis of the Secreted Proteins of the Parasite Haemonchus contortus Reveals Extensive Sequence Variation and Differential Immune Recognition

“…Post-translational modifications in the C-terminal tryptic peptide (as nearly all other peptides were resolved) or largely anomalous migration behavior can thus also contribute to this diversity. N-linked oligosaccharides of H. contortus have different structures in comparison to the host (24) and have been shown to contribute to immune recognition (25). In combination with the presence of gene families, as has been demonstrated for an Hc15 homologue of the nematode Cooperia punctata (26), this has clear implications for vaccination trials.…”

An antibody produced in tobacco expressing a hybrid β-1,4-galactosyltransferase is essentially devoid of plant carbohydrate epitopes

“…However, the galactose carrying N-glycans still contained the plant-specific ␤-1,2-xylose and ␣-1,3-Fuc residues linked to the core. These xylose (Xyl) and Fuc epitopes have been implicated in the allergenicity of certain plant and parasite proteins, which may pose a problem when plants are going to be used for the production of therapeutic mAbs (13)(14)(15).…”