A major continuous allergenic epitope of bovine β-lactoglobulin recognized by human IgE binding

• Published in: Clinical and experimental allergy Vol. 24; no. 8; pp. 758 - 764
• Main Authors: BALL, G., SHELTON, M. J., WALSH, B. J., HILL, D. J., HOSKING, C. S., HOWDEN, M. E. H.
• Format: Journal Article Conference Proceeding
• Language: English
• Published: Oxford, UK Blackwell Publishing Ltd 01.08.1994; Blackwell
• Subjects: Allergens - immunology; Allergic diseases; Amino Acid Sequence; Animals; Biological and medical sciences; Cattle; Child; Child, Preschool; Chromatography, Affinity; Enzyme-Linked Immunosorbent Assay; Epitope Mapping - methods; Epitopes - immunology; Female; Humans; Immunoglobulin E - immunology; Immunopathology; Infant; Lactoglobulins - immunology; Male; Medical sciences; Molecular Sequence Data; Other localizations; Radioimmunoassay; Human; Immunopathology; Allergy; Immunoglobulins; Milk protein; Antigenic determinant; Lactoglobulins; IgE; Cow milk; Child; ELISA assay; Allergen
• ISSN: 0954-7894; 1365-2222
• DOI: 10.1111/j.1365-2222.1994.tb00987.x

Summary Hexapeptides of sequential overlapping sequences of β‐lactoglobulin (BLG) were used to probe scrum from children with immediate‐type cow milk allergy for IgE binding to continuous epilopes of BLG in an enhanced enzyme‐linked immunosorbent assay (ELISA). Six regions of IgE binding were identified on the BLG molecule and these were synthesized as dodecapeptides. Inhibition of IgE binding to whole BLG was used to confirm the BLG‐specific binding of IgE to each of the synthesized peptides. One of the peptides. peptide 4, showed inhibition in an IgE anti‐BLG radioimmunoassay to all 16 sera tested. The patterns of inhibition with the native BLG molecule and peptide 4 were significantly correlated (P =0.005). suggesting that this peptide contains a major continuous IgE binding epitope of BLG.