Are Physicochemical Properties Shaping the Allergenic Potency of Plant Allergens?
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Are Physicochemical Properties Shaping the Allergenic Potency of Plant Allergens? Joana Costa 1 & Simona Lucia Bavaro 2,3 & Sara Benedé 4 & Araceli Diaz-Perales 5 & Cristina Bueno-Diaz 6 & Eva Gelencser 7 & Julia Klueber 8,9 & Colette Larré 10 & Daniel Lozano-Ojalvo 11 & Roberta Lupi 10 & Isabel Mafra 1 Gabriel Mazzucchelli 12 & Elena Molina 4 & Linda Monaci 2 & Laura Martín-Pedraza 13 & Cristian Piras 14,15 & Pedro M. Rodrigues 16 & Paola Roncada 17 & Denise Schrama 16 & Tanja Cirkovic-Velickovic 18,19,20 & Kitty Verhoeckx 21 & Caterina Villa 1 & Annette Kuehn 8 & Karin Hoffmann-Sommergruber 22 & Thomas Holzhauser 23
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# Springer Science+Business Media, LLC, part of Springer Nature 2020
Abstract 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. Keywords Plant allergens . Protein families . Allergenicity . Food processing . Matrix effect
Abbreviations ATI α-Amylase trypsin inhibitors BAT Basophil activation test DBPCFC Double-blind placebo-controlled food challenge EAST Enzyme allergosorbent test ELISA Enzyme-linked immunosorbent assay GMP Good manufacture practices HMW High molecular weight Electronic supplementary material The online version of this article (https://doi.org/10.1007/s12016-020-08810-9) contains supplementary material, which is available to authorized users. * Joana Costa [email protected] Extended author information av
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