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Research Project: Defining, Measuring, and Mitigating Attributes that Adversely Impact the Quality and Marketability of Foods

Location: Healthy Processed Foods Research

Title: Identification of almond (prunus dulcis) vicilin as a food allergen

Author
item Zhang, Yuzhu
item CHE, HUILIAN - China Agricultural University
item LYU, SHU-CHEN - Stanford University
item NADEAU, KARI - Stanford University
item McHugh, Tara

Submitted to: Journal of Allergy Clinical Immunology
Publication Type: Abstract Only
Publication Acceptance Date: 2/22/2019
Publication Date: 2/23/2019
Citation: Zhang, Y., Che, H., Lyu, S., Nadeau, K., Mchugh, T.H. 2019. Identification of almond (prunus dulcis) vicilin as a food allergen [abstract]. Journal of Allergy Clinical Immunology. 143(2):AB69. https://doi.org/10.1016/j.jaci.2018.12.210.
DOI: https://doi.org/10.1016/j.jaci.2018.12.210

Interpretive Summary:

Technical Abstract: Rationale: Four almond allergens have been officially designated by WHO/IUIS. In addition, a protein that recognized by at least one patient serum was reported to be Pru du 2S albumin. However, a recent report suggested that it might be Pru du vicilin. Vicilins from many species, including several tree nuts are known food allergens. We hypothesize that almond vicilin is a food allergen. Methods: Genomic DNA of the Nonpareil almond was isolated. The vicilin gene sequence was PCR amplified. The coding sequence of vicilin was determined and synthesized with codon optimization. Recombinant almond vicilin was expressed in E. coli and purified by FPLC. The recognition of the recombinant almond vicilin by IgE in sera from 18 subjects with almond allergy was analyzed by Western blot. Results: Most of the sera contained IgE specific to almond proteins yet to be identified. Twenty-seven percent of sera recognized the recombinant almond vicilin. Among these, some recognized both the N- and C-terminal domains of vicilin, while others only recognized one of the domains. Conclusions: Almond vicilin is a food allergen.