Definition of immunogenic carbohydrate epitopes

• Published in: Acta biochimica polonica Vol. 52; no. 3; pp. 629 - 632
• Main Authors: Paschinger, Katharina, Fabini, Gustáv, Schuster, David, Rendić, Dubravko, Wilson, Iain B H
• Format: Journal Article
• Language: English
• Published: Poland 01.01.2005
• Subjects: Allergens - chemistry; Allergens - genetics; Allergens - immunology; Animals; Caenorhabditis elegans - chemistry; Carbohydrate Sequence; Carbohydrates - chemistry; Carbohydrates - immunology; Cross Reactions; Drosophila melanogaster - chemistry; Epitopes - immunology; Fucose - chemistry; Fucosyltransferases - immunology; Horseradish Peroxidase - immunology; Humans; Immunoglobulin E - immunology; Molecular Sequence Data; Substrate Specificity
• ISSN: 0001-527X; 1734-154X
• DOI: 10.18388/abp.2005_3422

Carbohydrates are known as sources of immunological cross-reactivity of allergenic significance. In celery and in cypress pollen, the major allergens Api g 5 and Cup a 1 are recognised by antisera raised against anti-horseradish peroxidase and by patients' IgE which apparently bind carbohydrate epitopes; mass spectrometric analysis of the tryptic peptides and of their N-glycans showed the presence of oligosaccharides carrying both xylose and core alpha1,3-fucose residues. Core alpha1,3-fucose residues are also a feature of invertebrates: genetic and biochemical studies on the fruitfly Drosophila melanogaster, the parasitic trematode Schistosoma mansoni and the nematode worm Caenorhabditis elegans indicate that these organisms possess core alpha1,3-fucosyltransferases. Various experiments have shown that fucosyltransferases from both fly and worm are responsible in vivo and in vitro for the synthesis of N-glycans which cross-react with anti-horseradish peroxidase; thus, we can consider these enzymes as useful tools in generating standard compounds for testing cross-reactive carbohydrate epitopes of allergenic interest.