title: Studies on the aetiology of coeliac disease: no evidence for lectin-like components in wheat gluten.
abstract: In an approach to examine the lectin-hypothesis in the pathogenesis of coeliac disease, the presence of lectin-like components in three wheat gluten preparations known to induce coeliac disease, gliadin, Frazer fraction III and an acetic acid/ethanol extract of gluten, was investigated. Lectin-like components in these wheat gluten preparations were traced in binding studies employing a variety of model glycoproteins glycosylated with the different types of N-linked oligosaccharides, i.e., those of the high mannose-, complex- and hybrid-type. Binding affinity of wheat proteins to these glycoproteins was analyzed by affinity dotting and blotting techniques and was compared to that of the well characterized lectins Galanthus nivalis agglutinin, Concanavalin A and wheat germ agglutinin. Though the three wheat gluten preparations exhibited binding reactivity for distinct model glycoproteins, no correlation was found between the type of N-glycosylation of the model glycoproteins and their binding capability to the different wheat gluten preparations. Moreover, binding of the three gluten preparations to the model glycoproteins could not be inhibited by competitive saccharides (methyl-alpha-D-mannopyranoside, N-acetyl-D-glucosamine, mannan). Enzymatic deglycosylation of the ligand glycoproteins with endo-beta-N-acetylglucosaminidase H (Endo H, EC 3.2.1.96) or peptide N-glycosidase F (PNGase F, EC 3.5.1.52) abolished their binding reactivity for the plant lectins, but did not affect binding of the wheat gluten preparations. These results give no evidence for the presence of lectin-like components in wheat gluten preparations and do question the 'lectin hypothesis' of coeliac disease.
authors.affiliation: Institut für Klinische Chemie und Biochemie, Universitätsklinikum Rudolf Virchow, Berlin, Germany.
authors.forename: J
authors.initials: J
authors.lastname: Rühlmann
authors.forename: P
authors.initials: P
authors.lastname: Sinha
authors.forename: G
authors.initials: G
authors.lastname: Hansen
authors.forename: R
authors.initials: R
authors.lastname: Tauber
authors.forename: E
authors.initials: E
authors.lastname: Köttgen
mesh_terms: D000581:Amidohydrolases; D002446:Celiac Disease / Q000209:etiology*; D003208:Concanavalin A / Q000378:metabolism; D027801:Galanthus; D005903:Gliadin / Q000009:adverse effects / Q000378:metabolism*; D005983:Glutens / Q000009:adverse effects / Q000378:metabolism*; D006023:Glycoproteins / Q000378:metabolism*; D006031:Glycosylation; D006596:Hexosaminidases; D006801:Humans; D007413:Intestinal Mucosa / Q000378:metabolism*; D037102:Lectins / Q000378:metabolism*; D017038:Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase; D009844:Oligosaccharides / Q000032:analysis; D010434:Pepsin A; D043524:Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase; D037121:Plant Lectins; D014908:Triticum / Q000009:adverse effects*; D014357:Trypsin
chemical_list: D006023:Glycoproteins; D037102:Lectins; D009844:Oligosaccharides; D037121:Plant Lectins; D003208:Concanavalin A; D005983:Glutens; D005903:Gliadin; D006596:Hexosaminidases; D017038:Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase; D014357:Trypsin; D010434:Pepsin A; D000581:Amidohydrolases; D043524:Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase