Are Physicochemical Properties Shaping the Allergenic Potency of Plant Allergens?

Joana Costa*, Simona Lucia Bavaro, Sara Benedé, Araceli Diaz-Perales, Cristina Bueno-Diaz, Eva Gelencser, Julia Klueber, Colette Larré, Daniel Lozano-Ojalvo, Roberta Lupi, Isabel Mafra, Gabriel Mazzucchelli, Elena Molina, Linda Monaci, Laura Martín-Pedraza, Cristian Piras, Pedro M. Rodrigues, Paola Roncada, Denise Schrama, Tanja Cirkovic-VelickovicKitty Verhoeckx, Caterina Villa, Annette Kuehn, Karin Hoffmann-Sommergruber, Thomas Holzhauser

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

98 Citations (Scopus)


This review searched for published evidence that could explain how different physicochemical properties impact on the allergenicity of food proteins and if their effects would follow specific patterns among distinct protein families. Owing to the amount and complexity of the collected information, this literature overview was divided in two articles, the current one dedicated to protein families of plant allergens and a second one focused on animal allergens. Our extensive analysis of the available literature revealed that physicochemical characteristics had consistent effects on protein allergenicity for allergens belonging to the same protein family. For example, protein aggregation contributes to increased allergenicity of 2S albumins, while for legumins and cereal prolamins, the same phenomenon leads to a reduction. Molecular stability, related to structural resistance to heat and proteolysis, was identified as the most common feature promoting plant protein allergenicity, although it fails to explain the potency of some unstable allergens (e.g. pollen-related food allergens). Furthermore, data on physicochemical characteristics translating into clinical effects are limited, mainly because most studies are focused on in vitro IgE binding. Clinical data assessing how these parameters affect the development and clinical manifestation of allergies is minimal, with only few reports evaluating the sensitising capacity of modified proteins (addressing different physicochemical properties) in murine allergy models. In vivo testing of modified pure proteins by SPT or DBPCFC is scarce. At this stage, a systematic approach to link the physicochemical properties with clinical plant allergenicity in real-life scenarios is still missing.

Original languageEnglish
Pages (from-to)37-63
Number of pages27
JournalClinical Reviews in Allergy and Immunology
Issue number1
Publication statusPublished - Feb 2022


  • Allergenicity
  • Food processing
  • Matrix effect
  • Plant allergens
  • Protein families


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