Ara h 6 complements Ara h 2 as an important marker for IgE reactivity to peanut

Audrey E. Koid; Martin D. Chapman; Robert G. Hamilton; Ronald Van Ree; Serge A. Versteeg; Stephen C. Dreskin; Stef J. Koppelman; Sabina Wünschmann

doi:10.1021/jf4022509

Ara h 6 complements Ara h 2 as an important marker for IgE reactivity to peanut

Audrey E. Koid, Martin D. Chapman, Robert G. Hamilton, Ronald Van Ree, Serge A. Versteeg, Stephen C. Dreskin, Stef J. Koppelman, Sabina Wünschmann

School of Medicine

Research output: Contribution to journal › Article › peer-review

31 Scopus citations

Abstract

The similarities of two major peanut allergens, Ara h 2 and Ara h 6, in molecular size, amino acid sequence, and structure have made it difficult to obtain natural Ara h 6 free of Ara h 2. The objectives of this study were to purify natural Ara h 6 that is essentially free of Ara h 2 and to compare its IgE reactivity and potency in histamine release assays to Ara h 2. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the highly purified allergen (<0.01% Ara h 2) revealed a single 14.5 kD band, and the identity of Ara h 6 was confirmed by liquid chromatography-tandem mass spectrometry. Ara h 6 showed a higher seroprevalence in chimeric IgE enzyme-linked immunosorbent assay (n = 54) but a weaker biological activity in basophil histamine release assays than Ara h 2. Purified Ara h 6 will be useful for diagnostic IgE antibody assays as well as molecular and cellular studies to investigate the immunological mechanisms of peanut allergy.

Original language	English (US)
Pages (from-to)	206-213
Number of pages	8
Journal	Journal of Agricultural and Food Chemistry
Volume	62
Issue number	1
DOIs	https://doi.org/10.1021/jf4022509
State	Published - Jan 8 2014

Keywords

IgE reactivity
allergen
histamine release
peanut

ASJC Scopus subject areas

Chemistry(all)
Agricultural and Biological Sciences(all)

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10.1021/jf4022509

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title = "Ara h 6 complements Ara h 2 as an important marker for IgE reactivity to peanut",

abstract = "The similarities of two major peanut allergens, Ara h 2 and Ara h 6, in molecular size, amino acid sequence, and structure have made it difficult to obtain natural Ara h 6 free of Ara h 2. The objectives of this study were to purify natural Ara h 6 that is essentially free of Ara h 2 and to compare its IgE reactivity and potency in histamine release assays to Ara h 2. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the highly purified allergen (<0.01% Ara h 2) revealed a single 14.5 kD band, and the identity of Ara h 6 was confirmed by liquid chromatography-tandem mass spectrometry. Ara h 6 showed a higher seroprevalence in chimeric IgE enzyme-linked immunosorbent assay (n = 54) but a weaker biological activity in basophil histamine release assays than Ara h 2. Purified Ara h 6 will be useful for diagnostic IgE antibody assays as well as molecular and cellular studies to investigate the immunological mechanisms of peanut allergy.",

keywords = "IgE reactivity, allergen, histamine release, peanut",

author = "Koid, {Audrey E.} and Chapman, {Martin D.} and Hamilton, {Robert G.} and {Van Ree}, Ronald and Versteeg, {Serge A.} and Dreskin, {Stephen C.} and Koppelman, {Stef J.} and Sabina W{\"u}nschmann",

year = "2014",

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day = "8",

doi = "10.1021/jf4022509",

language = "English (US)",

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AU - Koid, Audrey E.

AU - Chapman, Martin D.

AU - Hamilton, Robert G.

AU - Van Ree, Ronald

AU - Versteeg, Serge A.

AU - Dreskin, Stephen C.

AU - Koppelman, Stef J.

AU - Wünschmann, Sabina

PY - 2014/1/8

Y1 - 2014/1/8

N2 - The similarities of two major peanut allergens, Ara h 2 and Ara h 6, in molecular size, amino acid sequence, and structure have made it difficult to obtain natural Ara h 6 free of Ara h 2. The objectives of this study were to purify natural Ara h 6 that is essentially free of Ara h 2 and to compare its IgE reactivity and potency in histamine release assays to Ara h 2. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the highly purified allergen (<0.01% Ara h 2) revealed a single 14.5 kD band, and the identity of Ara h 6 was confirmed by liquid chromatography-tandem mass spectrometry. Ara h 6 showed a higher seroprevalence in chimeric IgE enzyme-linked immunosorbent assay (n = 54) but a weaker biological activity in basophil histamine release assays than Ara h 2. Purified Ara h 6 will be useful for diagnostic IgE antibody assays as well as molecular and cellular studies to investigate the immunological mechanisms of peanut allergy.

AB - The similarities of two major peanut allergens, Ara h 2 and Ara h 6, in molecular size, amino acid sequence, and structure have made it difficult to obtain natural Ara h 6 free of Ara h 2. The objectives of this study were to purify natural Ara h 6 that is essentially free of Ara h 2 and to compare its IgE reactivity and potency in histamine release assays to Ara h 2. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the highly purified allergen (<0.01% Ara h 2) revealed a single 14.5 kD band, and the identity of Ara h 6 was confirmed by liquid chromatography-tandem mass spectrometry. Ara h 6 showed a higher seroprevalence in chimeric IgE enzyme-linked immunosorbent assay (n = 54) but a weaker biological activity in basophil histamine release assays than Ara h 2. Purified Ara h 6 will be useful for diagnostic IgE antibody assays as well as molecular and cellular studies to investigate the immunological mechanisms of peanut allergy.

KW - IgE reactivity

KW - allergen

KW - histamine release

KW - peanut

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Ara h 6 complements Ara h 2 as an important marker for IgE reactivity to peanut

Abstract

Keywords

ASJC Scopus subject areas

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