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

G. Ball, M. J. Shelton*, B. J. Walsh, D. J. Hill, C. S. Hosking, M. E H Howden

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

109 Citations (Scopus)

Abstract

Hexapeptides of sequential overlapping sequences of β-lactoglobulin (BLG) were used to probe serum from children with immediate-type cow milk allergy for IgE binding to continuous epitopes 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.

Original languageEnglish
Pages (from-to)758-764
Number of pages7
JournalClinical and Experimental Allergy
Volume24
Issue number8
DOIs
Publication statusPublished - 1994
Externally publishedYes

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