Ranking primary food allergens by specific IgE-binding and clinical relevance in Dutch adults to identify reference protein sets for allergenicity assessment.

The increasing introduction of novel protein sources globally requires more robust allergenicity evaluations to predict their sensitising capacity. This study ranked plant-derived and animal-derived food allergens to establish reference proteins that may support the future development of predictive tools for de novo sensitisation. Sera from 307 Dutch adult patients presenting with suspected food allergy at an allergology outpatient clinic were analysed with Allergy Xplorer2 multiplex immunoassay. Food components were ranked based on specific IgE-binding frequencies, intensities, and clinical relevance. Plant-derived components demonstrated higher overall positive frequencies (491 vs 122) and median intensities (2.2 vs 1.7 kUA/L) than animal-derived components. Within plant protein families, 2S albumins exhibited the highest frequencies (197) and median intensities (4.2 kUA/L); with peanut allergens rAra h 2 (10.0%, 4.5 kUA/L) and rAra h 6 (9.4%, 7.1 kUA/L) most prominent and clinically relevant. Considering overall ranking, a proposed plant-derived reference panel comprises strong (Ara h 2, Jug r 4), intermediate (Ses i 1, Pru p 3), and weak (Gly m 5, Sin a 1) sensitising proteins. Plant-family ranking appears most effective for establishing reference sets, highlighting their potential utility in future allergenicity risk assessment frameworks tailored to clinical relevance of specific food items and novel protein sources.