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:https://doi.org/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

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

40 Citations (Scopus)

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
Pages (from-to)	206-213
Journal	Journal of agricultural and food chemistry
Volume	62
Issue number	1
DOIs	https://doi.org/10.1021/jf4022509
Publication status	Published - 2014

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https://doi.org/10.1021/jf4022509

Cite this

@article{3e099ea788f34b7f947e42f6c9abbdab,

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",

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",

doi = "https://doi.org/10.1021/jf4022509",

language = "English",

volume = "62",

pages = "206--213",

journal = "Journal of agricultural and food chemistry",

issn = "0021-8561",

publisher = "American Chemical Society",

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TY - JOUR

T1 - Ara h 6 complements Ara h 2 as an important marker for IgE reactivity to peanut

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

Y1 - 2014

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

U2 - https://doi.org/10.1021/jf4022509

DO - https://doi.org/10.1021/jf4022509

M3 - Article

C2 - 24328145

SN - 0021-8561

VL - 62

SP - 206

EP - 213

JO - Journal of agricultural and food chemistry

JF - Journal of agricultural and food chemistry

IS - 1

ER -