| Literature DB >> 34037388 |
Danijela Apostolovic1, Justin T Marsh2, Joe Baumert2, Steve L Taylor2, Adrie Westphal3, Harmen de Jongh4, Phil Johnson2, Govardus A H de Jong5, Stef J Koppelman2.
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.Entities:
Keywords: 2S albumin; Ara h 7; Arachis hypogaea; allergen; peanuts
Mesh:
Substances:
Year: 2021 PMID: 34037388 DOI: 10.1021/acs.jafc.1c00618
Source DB: PubMed Journal: J Agric Food Chem ISSN: 0021-8561 Impact factor: 5.279