N- and O-linked oligosaccharides of allergenic glycoproteins

Glycoconj J. 2001 May;18(5):373-90. doi: 10.1023/a:1014860030380.

Abstract

Cross-linking of cell-bound IgE on mast cells or basophils by polyvalent antigens causes the release of histamine and other mediators of the allergic response which then lead to the development of allergic symptoms. In this event not only peptide epitopes, but also carbohydrates can act as cross-linking elements. Since peptide epitopes of allergens are subject of most published studies, this review is focused on glycosidic epitopes. The current knowledge of the structures and possible epitopes of oligosaccharides linked to allergenic glycoproteins is briefly reviewed, showing that complex plant N-glycans containing alpha1,3 fucose and beta1,2 xylose are most frequently involved in the structures of IgE epitopes. In own studies a prevalence of up to 29% anti-glycan IgE was determined among pollen-allergic patients. The clinical relevance of these carbohydrate specific IgE antibodies is still a matter of controversial discussions.

Publication types

  • Review

MeSH terms

  • Allergens / chemistry*
  • Animals
  • Carbohydrate Conformation
  • Carbohydrate Sequence
  • Epitopes / chemistry
  • Epitopes / immunology
  • Glycoproteins / chemistry*
  • Glycoproteins / immunology*
  • Humans
  • Immunoglobulin E / immunology
  • Models, Molecular
  • Molecular Sequence Data
  • Oligosaccharides / chemistry*
  • Oligosaccharides / immunology
  • Protein Conformation

Substances

  • Allergens
  • Epitopes
  • Glycoproteins
  • Oligosaccharides
  • Immunoglobulin E