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

doi:10.1111/j.1365-2222.1994.tb00987.x

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 journal › Article › peer-review

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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 language	English
Pages (from-to)	758-764
Number of pages	7
Journal	Clinical and Experimental Allergy
Volume	24
Issue number	8
DOIs	https://doi.org/10.1111/j.1365-2222.1994.tb00987.x
Publication status	Published - 1994
Externally published	Yes

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10.1111/j.1365-2222.1994.tb00987.x

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title = "A major continuous allergenic epitope of bovine β-lactoglobulin recognized by human IgE binding",

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.",

author = "G. Ball and Shelton, {M. J.} and Walsh, {B. J.} and Hill, {D. J.} and Hosking, {C. S.} and Howden, {M. E H}",

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T1 - A major continuous allergenic epitope of bovine β-lactoglobulin recognized by human IgE binding

AU - Ball, G.

AU - Shelton, M. J.

AU - Walsh, B. J.

AU - Hill, D. J.

AU - Hosking, C. S.

AU - Howden, M. E H

PY - 1994

Y1 - 1994

N2 - 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.

AB - 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.

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DO - 10.1111/j.1365-2222.1994.tb00987.x

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JO - Clinical and Experimental Allergy

JF - Clinical and Experimental Allergy

IS - 8

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

Abstract

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