Joana Costa, Caterina Villa, Kitty Verhoeckx, Tanja Cirkovic-Velickovic, Denise Schrama, Paola Roncada, Pedro M. Rodrigues, Cristian Piras, Laura Martín-Pedraza, Linda Monaci, Elena Molina, Gabriel Mazzucchelli, Isabel Mafra, Roberta Lupi, Daniel Lozano-Ojalvo, Colette Larré, Julia Klueber, Eva Gelencser, Cristina Bueno-Diaz, Araceli Diaz-Perales, Sara Benedé, Simona Lucia Bavaro, Annette Kuehn, Karin Hoffmann-Sommergruber, Thomas Holzhauser, University of Coimbra [Portugal] (UC), TNO, University of Belgrade [Belgrade], Universidade do Algarve (UAlg), Università degli Studi 'Magna Graecia' di Catanzaro [Catanzaro, Italie] (UMG), Laboratoire d'Énergétique Moléculaire et Macroscopique, Combustion (EM2C), Université Paris Saclay (COmUE)-Centre National de la Recherche Scientifique (CNRS)-CentraleSupélec, Department of Chemistry, University of Reading (UOR), Universidad Complutense de Madrid = Complutense University of Madrid [Madrid] (UCM), Institute of Sciences of Food Production (ISPA), Consiglio Nazionale delle Ricerche (CNR), Instituto de Investigación en Ciencias de la Alimentación (CIAL), Laboratory of Mass Spectrometry-GIGA-Proteomics, Université de Liège, Departamento de Quimica (REQUIMTE), Universidade de Lisboa (ULISBOA)-Centro de Quimica Fina e Biotecnologia, Unité de recherche sur les Biopolymères, Interactions Assemblages (BIA), Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Icahn School of Medicine at Mount Sinai, Partenaires INRAE, Luxembourg Institute of Health (LIH), Plant Protection Institute [Budapest] (ATK NOVI), Centre for Agricultural Research [Budapest] (ATK), Hungarian Academy of Sciences (MTA)-Hungarian Academy of Sciences (MTA), Centro de Biotecnologia y Genomica de Plantas - Centre for Plant Biotechnology and Genomics, Teagasc Food Research Centre [Fermoy, Ireland], Medizinische Universität Wien = Medical University of Vienna, Paul-Ehrlich-Institute - Federal Institute for Vaccines and Biomedicines (EPI), European Project, European Project: 650006,H2020,H2020-SMEINST-1-2014,PROFIT(2014), European Commission, European Cooperation in Science and Technology, Fundação para a Ciência e a Tecnologia (Portugal), Ministry of Education, Science and Technological Development (Serbia), Ministério da Ciência, Tecnologia e Ensino Superior (Portugal), Fonds National de la Recherche Luxembourg, Università degli Studi 'Magna Graecia' di Catanzaro = University of Catanzaro (UMG), CentraleSupélec-Centre National de la Recherche Scientifique (CNRS)-Université Paris Saclay (COmUE), National Research Council of Italy | Consiglio Nazionale delle Ricerche (CNR), and Universidade de Lisboa = University of Lisbon (ULISBOA)-Centro de Quimica Fina e Biotecnologia
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. 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., 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).