Abstract
2S albumins are important peanut allergens. Within this protein family, Ara h 2 and Ara h 6 have been described in detail, but Ara h 7 has received little attention. We now describe the first purification of Ara h 7 and its characterization. Two Ara h 7 isoforms were purified from peanuts. Mass spectrometry revealed that both the isoforms have a post-translation cleavage, a hydroxyproline modification near the N-terminus, and four disulfide bonds. The secondary structure of both Ara h 7 isoforms is highly comparable to those of Ara h 2 and Ara h 6. Both Ara h 7 isoforms bind IgE, and Ara h 7 is capable of inhibiting the binding between Ara h 2 and IgE, suggesting at least partially cross-reactive IgE epitopes. Ara h 7 was found in all main market types of peanut, at comparable levels. This suggests that Ara h 7 is a relevant allergen from the peanut 2S albumin protein family.
Original language | English (US) |
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Pages (from-to) | 6318-6329 |
Number of pages | 12 |
Journal | Journal of Agricultural and Food Chemistry |
Volume | 69 |
Issue number | 22 |
DOIs | |
State | Published - Jun 9 2021 |
Keywords
- 2S albumin
- Ara h 7
- Arachis hypogaea
- allergen
- peanuts
ASJC Scopus subject areas
- General Chemistry
- General Agricultural and Biological Sciences