Ara h 6 Complements Ara h 2 as an Important Marker for IgE Reactivity to Peanut

Authors

Audrey E. Koid, INDOOR Biotechnologies, Inc.
Martin D. Chapman, INDOOR Biotechnologies, Inc.
Robert G. Hamilton, Johns Hopkins University School of Medicine
Ronald van Ree, Academic Medical Center
Serge A. Versteeg, Academic Medical Center
Stephen C. Dreskin, University of Colorado Denver
Stef J. Koppelman, University of Nebraska-LincolnFollow
Sabina Wünschmann, INDOOR Biotechnologies, Inc.

Document Type

Article

Date of this Version

1-8-2014

Citation

J Agric Food Chem. 2014 January 8; 62(1): 206–213. doi:10.1021/jf4022509.

Comments

Copyright 2014 American Chemical Society. Used by permission.

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. SDS-PAGE of the highly purified allergen (<0.01% Ara h 2) revealed a single 14.5kD band and the identity of Ara h 6 was confirmed by LC-MS/MS. Ara h 6 showed a higher seroprevalence in chimeric-IgE ELISA (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.