Specificities of monoclonal antibodies to domain I of alpha-gliadins.
Eight monoclonal antibodies were raised against a sequenced 54-amino-acid peptide of alpha-gliadin, which is thought to exacerbate coeliac disease. Five of the antibodies cross-reacted with coeliac non-toxic cereals. Two of eight of the antibodies bound specifically to coeliac toxic prolamins. These two antibodies cross-reacted with high molecular weight gliadins, which are closely related to alpha-gliadins and whose toxicity to patients with coeliac disease is unclear. The antibodies were screened by enzyme-linked immunosorbent assay against three amino-acid-sequenced peptides of alpha-gliadin with single amino-acid differences. Differential binding of antibody WC2 suggested that this antibody binds in the region of amino-acid residue 36, a proline residue, where there may be an antigenic beta-reverse turn. This proline residue forms part of a tetrapeptide motif, QQQP, which is thought to be present in all coeliac-active peptides.
Ellis
H J
HJ
Rayne Institute, St. Thomas' Hospital, London, U.K.
Doyle
A P
AP
Wieser
H
H
Sturgess
R P
RP
Ciclitira
P J
PJ
D000818:Animals; D000911:Antibodies, Monoclonal / Q000276:immunology*; D000918:Antibody Specificity; D003429:Cross Reactions; D002523:Edible Grain / Q000276:immunology; D004797:Enzyme-Linked Immunosorbent Assay; D005903:Gliadin / Q000235:genetics* / Q000276:immunology; D007114:Immunization; D015151:Immunoblotting; D051379:Mice; D008807:Mice, Inbred BALB C; D010940:Plant Proteins / Q000276:immunology; D055315:Prolamins
D000911:Antibodies, Monoclonal; D010940:Plant Proteins; D055315:Prolamins; D005903:Gliadin