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.
Highlights
Ara h 6 has a reported seroprevalence similar to Ara h 2, a major peanut allergen
The objective of this study was to obtain purified 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
Natural Ara h 6 was purified from peanut flour extract by affinity chromatography and size exclusion chromatography
Summary
Ara h 6 has a reported seroprevalence similar to Ara h 2, a major peanut allergen. Both allergens are of similar molecular size and share 50% identity in their amino acid sequences. Their similarity has made it difficult to obtain natural Ara h 6 free of Ara h 2 for immunoreactivity studies. The objective of this study was to obtain purified 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
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