Are Physicochemical Properties Shaping the Allergenic Potency of Animal Allergens?
Costa, Joana; Villa, Caterina; Verhoeckx, Kitty; Cirkovic-Velickovic, Tanja; Schrama, Denise; Roncada, Paola; Rodrigues, Pedro M.; Piras, Cristian; Martín-Pedraza, Laura; Monaci, Linda; Molina, Elena; Mazzucchelli, Gabriel; Mafra, Isabel; Lupi, Roberta; Lozano-Ojalvo, Daniel; Larré, Colette; Klueber, Julia; Gelencser, Eva; Bueno-Diaz, Cristina; Diaz-Perales, Araceli; Benedé, Sara; Bavaro, Simona Lucia; Kuehn, Annette; Hoffmann-Sommergruber, Karin; Holzhauser, Thomas
(2022) Clinical Reviews in Allergy and Immunology, volume 62, issue 1, pp. 1 - 36
(Article)
Abstract
Key determinants for the development of an allergic response to an otherwise ‘harmless’ food protein involve different factors like the predisposition of the individual, the timing, the dose, the route of exposure, the intrinsic properties of the allergen, the food matrix (e.g. lipids) and the allergen modification by food processing.
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Various physicochemical parameters can have an impact on the allergenicity of animal proteins. Following our previous review on how physicochemical parameters shape plant protein allergenicity, the same analysis was proceeded here for animal allergens. We found that each parameter can have variable effects, ranging on an axis from allergenicity enhancement to resolution, depending on its nature and the allergen. While glycosylation and phosphorylation are common, both are not universal traits of animal allergens. High molecular structures can favour allergenicity, but structural loss and uncovering hidden epitopes can also have a similar impact. We discovered that there are important knowledge gaps in regard to physicochemical parameters shaping protein allergenicity both from animal and plant origin, mainly because the comparability of the data is poor. Future biomolecular studies of exhaustive, standardised design together with strong validation part in the clinical context, together with data integration model systems will be needed to unravel causal relationships between physicochemical properties and the basis of protein allergenicity.
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Keywords: Allergen integrity, Allergenicity, Animal allergens, Food processing, Protein families, Immunology and Allergy
ISSN: 1080-0549
Publisher: Humana Press
Note: Funding Information: The authors highly appreciate the support from the COST Office. This article is based upon work from COST Action FA1402, supported by COST (European Cooperation in Science and Technology, www.cost.eu ). This work was also supported by Fundação para a Ciência e Tecnologia under the Partnership Agreement UIDB 50006/2020 and by the projects AlleRiskAssess—PTDC/BAA-AGR/31720/2017. C.V. is grateful to FCT grant (PD/BD/114576/2016) financed by POPH-QREN (subsidised by FSE and MCTES). J.C. acknowledges FCT for the research contract (SFRH/BPD/102404/2014). T.C.V. is grateful to the Ministry of Education, Science and Technological Development of the Republic of Serbia through grant number OI172024. P.M.R. and D.S. are grateful to FCT through project UIDB/04326/2020 and Mar2020 16-02-01-FMP-0014—“ALLYFISH”. J.K. and A.K. acknowledge PRIDE program grants (PRIDE/11012546/NEXTIMMUNE). J.K. also acknowledges FNR (Fonds National de la Recherche) and the PMC (Personalised Medicine Consortium). Publisher Copyright: © 2021, Springer Science+Business Media, LLC, part of Springer Nature.
(Peer reviewed)