4.7 Article

Purification and Initial Characterization of Ara h 7, a Peanut Allergen from the 2S Albumin Protein Family

Journal

JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
Volume 69, Issue 22, Pages 6318-6329

Publisher

AMER CHEMICAL SOC
DOI: 10.1021/acs.jafc.1c00618

Keywords

peanuts; Arachis hypogaea; 2S albumin; allergen; Ara h 7

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Ara h 7, an important peanut allergen from the 2S albumin protein family, has been purified and characterized, showing unique features and presence in all main market types of peanuts.
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.

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