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A random phage heptapeptide library was screened with rabbit antibodies against wheat flour proteins comprising gliadins and a small amount of low molecular weight glutenins (gli/glu). Gli/glu antibodies isolated from the sera selected different consensus sequences (CS). All CS contained tri- to pentapeptide stretches homologous to gli/glu sequences (proposed epitopes). In alpha- and gamma-type gliadins, these sequences are clustered in the N-terminal region recently suspected to be toxic for humans with celiac disease. Peptides with CS were synthesized and checked for reactivity. Only immune and no control rabbit sera reacted with synthetic peptides. One of eight human sera containing gliadin antibodies was reactive as well (4/8 peptides) but control sera were negative. Thus the phage display technique is useful for epitope screening of polyclonal antibodies even in the case of a group of homologous but diverse antigens.

Type

Journal article

Journal

FEBS Lett

Publication Date

14/08/1998

Volume

433

Pages

103 - 107

Keywords

Amino Acid Sequence, Animals, Antibodies, Bacteriophages, Consensus Sequence, Enzyme-Linked Immunosorbent Assay, Epitopes, Gliadin, Haplorhini, Humans, Immunoblotting, Molecular Weight, Peptide Fragments, Peptide Library, Rabbits