{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Kabasser S"],"funding":["Austrian Science Fund FWF","Medical University of Vienna"],"pagination":["131028"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7614219"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["370"],"pubmed_abstract":["Macadamia nut is an increasingly popular food item of a healthy diet. However, macadamia nut is also a potent allergenic food. To date, there is little information about the allergenic proteins involved. In this study, using sera from macadamia nut allergic individuals, four IgE-binding proteins were detected. Their identities were determined by tandem mass spectrometry with de novo sequencing. Three IgE-reactive proteins, the vicilin Mac i 1, the legumin Mac i 2 and the antimicrobial peptide 2a/Mac i 1 (28-76) were purified from the nut while the non-specific lipid transfer protein was produced as a recombinant in Pichia pastoris. IgE-binding assays using sera from well-characterized groups of tree nut and/or peanut allergic patients revealed that the allergens were mainly recognized by s"],"journal":["Food chemistry"],"pubmed_title":["Identification of vicilin, legumin and antimicrobial peptide 2a as macadamia nut allergens."],"pmcid":["PMC7614219"],"funding_grant_id":["W 1248","P 30936-B30","P 30936"],"pubmed_authors":["Breiteneder H","Taki AC","Koplin J","Hummel K","Kamath S","Pratap K","Kabasser S","Perrett K","Lopata AL","Dang T","Radauer C","Bublin M"],"additional_accession":[]},"is_claimable":false,"name":"Identification of vicilin, legumin and antimicrobial peptide 2a as macadamia nut allergens.","description":"Macadamia nut is an increasingly popular food item of a healthy diet. However, macadamia nut is also a potent allergenic food. To date, there is little information about the allergenic proteins involved. In this study, using sera from macadamia nut allergic individuals, four IgE-binding proteins were detected. Their identities were determined by tandem mass spectrometry with de novo sequencing. Three IgE-reactive proteins, the vicilin Mac i 1, the legumin Mac i 2 and the antimicrobial peptide 2a/Mac i 1 (28-76) were purified from the nut while the non-specific lipid transfer protein was produced as a recombinant in Pichia pastoris. IgE-binding assays using sera from well-characterized groups of tree nut and/or peanut allergic patients revealed that the allergens were mainly recognized by s","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Feb","modification":"2026-05-28T17:46:45.833Z","creation":"2025-04-04T11:27:08.084Z"},"accession":"S-EPMC7614219","cross_references":{"pubmed":["34525424"],"doi":["10.1016/j.foodchem.2021.131028"]}}