The DOI matches its Crossref record; 119 of the 119 references it cites were found in a registry or an index.
Molecular properties of food allergens
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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“Furthermore, the carbohydrate chains normally exert a stabilizing effect on protein structure, offering protection towards processing and/or gastroduodenal digestion and thus contributing to the allergenic potential [11].”
From Influence of the Carbohydrate Moieties on the Immunoreactivity and Digestibility of the Egg Allergen Ovomucoid (2013) · cites this paper as [11]
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“In addition, differences in epitope accessibility, despite sequence similarity, may reduce effective IgE cross-linking (Breiteneder and Mills 2005; Sicherer and Sampson 2014; Kruse et al. 2021).”
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Metadata
- Authors
- Breiteneder, H., & Mills, E. N. C.
- Affiliations
- Medical University of Vienna (AT)
- Quadram Institute (GB)
- Corresponding author
- Breiteneder, Heimo
- 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)
- 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
- 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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