Cited by 359Food Allergy and Anaphylaxis ResearchAllergic Rhinitis and SensitizationProteins in Food Systems

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Molecular properties of food allergens

Breiteneder, Heimo, Mills, E.N. Clare·2005·Journal of Allergy and Clinical Immunology

DOI 10.1016/j.jaci.2004.10.022

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Abstract

Plant food allergens belong to a rather limited number of protein families and are also characterized by a number of biochemical and physicochemical properties, many of which are also shared by food allergens of animal origin. These include thermal stability and resistance to proteolysis, which are enhanced by an ability to bind ligands, such as metal ions, lipids, or steroids. Other types of lipid interaction, including membranes or other lipid structures, represent another feature that might promote the allergenic properties of certain food proteins. A structural feature clearly related to stability is intramolecular disulfide bonds alongside posttranslational modifications, such as N-glycosylation. Some plant food allergens, such as the cereal seed storage prolamins, are rheomorphic proteins with polypeptide chains that adopt an ensemble of secondary structures resembling unfolded or partially folded proteins. Other plant food allergens are characterized by the presence of repetitive structures, the ability to form oligomers, and the tendency to aggregate. A summary of our current knowledge regarding the molecular properties of food allergens is presented. Although we cannot as yet predict the allergenicity of a given food protein, understanding of the molecular properties that might predispose them to becoming allergens is an important first step and will undoubtedly contribute to the integrative allergenic risk assessment process being adopted by regulators.

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EAACI Molecular Allergology User's Guide
Matricardi, P. M., Kleine‐Tebbe, J., Hoffmann, H. J., Valenta, R., Hilger, C., Hofmaier, S., Aalberse, R. C., Agache, I., Asero, R., Ballmer‐Weber, B., et al. (2016) · Pediatric Allergy and Immunology · doi:10.1111/pai.12563 · Cited by 932
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“In contrast, common structural features have been established for food allergens that sensitize through the gastrointestinal tract.(24) These features, such as high numbers of disulfide bonds, repetitive structures, binding of lipid or metal ions, and formation of stable oligomers, confer stability toward heat, acid,…”
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Authors: Breiteneder, H., & Mills, E. N. C.
Affiliations: Medical University of Vienna (AT)
Quadram Institute (GB)
Corresponding author: Breiteneder, Heimo
ORCID: Breiteneder, Heimo
Mills, E.N. Clare
Venue: Journal of Allergy and Clinical Immunology
Publisher: Elsevier BV
Published: 2005-01
Volume: 115
Issue: 1
Pages: 14-23
ISSN: 0091-6749 (ISSN-L)
DOI: 10.1016/j.jaci.2004.10.022
OpenAlex: W2043345697
Cited by: 359
References: 119
Citations by year: 2026: 7 · 2025: 16 · 2024: 14 · 2023: 14 · 2022: 11 · 2021: 18 · 2020: 18 · 2019: 6 · 2018: 14 · 2017: 16 · 2016: 16 · 2015: 21 · 2014: 18 · 2013: 19 · 2012: 26
FWCI: 2.79
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
Locations: Journal of Allergy and Clinical Immunology (publishedVersion)
PubMed (publishedVersion)
Topics: Health Sciences › Medicine › Immunology and Allergy › Food Allergy and Anaphylaxis Research
Health Sciences › Medicine › Immunology and Allergy › Allergic Rhinitis and Sensitization
Life Sciences › Agricultural and Biological Sciences › Food Science › Proteins in Food Systems
Keywords: food allergens, plant food allergens, protein stability, thermal stability, protease resistance, metal ion binding, lipid binding, membrane binding, disulfide bonds, N-glycosylation, seed storage proteins, prolamin, protein secondary structure, protein aggregation, allergenicity prediction
MeSH terms: Allergens, Animals, Cell Membrane, Food Hypersensitivity, Glycosylation, Humans, Ligands, Metals, Protein Binding, Steroids, Temperature, Plant Proteins, Dietary, Protein Structure, Secondary, Protein Structure, Tertiary, Lipid Metabolism

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