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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Burks, A. W., James, J. M., & Eigenmann, P. (1951) · Cited by 2,573
Intrinsically disordered protein
Dunker, A. K., Lawson, J. D., Brown, C. J., Williams, R. M., Romero, P., Oh, J. S., Oldfield, C. J., Campen, A. M., Ratliff, C. M., Hipps, K. W., et al. (2001) · Journal of Molecular Graphics and Modelling · doi:10.1016/s1093-3263(00)00138-8 · Cited by 2,272
Intrinsically Disordered Proteins
Uversky, V. N. (2013) · Elsevier eBooks · doi:10.1016/b978-0-12-374984-0.01698-3 · Cited by 1,646
Mechanism of protein stabilization by glycerol: preferential hydration in glycerol-water mixtures
Gekko, K., & Timasheff, S. N. (1981) · Biochemistry · doi:10.1021/bi00519a023 · Cited by 1,185
Phospholipids in animal eukaryotic membranes: transverse asymmetry and movement
Zachowski, A. (1993) · Biochemical Journal · doi:10.1042/bj2940001 · Cited by 858
Update on food allergy.
Sampson, H. (2004) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2004.03.014 · Cited by 844
Food allergy. Part 1: Immunopathogenesis and clinical disorders
Sampson, H. A. (1999) · Journal of Allergy and Clinical Immunology · doi:10.1016/s0091-6749(99)70411-2 · Cited by 828
Structural biology of allergens
Aalberse, R. C. (2000) · Journal of Allergy and Clinical Immunology · doi:10.1067/mai.2000.108434 · Cited by 671
Calcium binding and conformational response in EF-hand proteins
Ikura, M. (1996) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(06)80021-6 · Cited by 664
9. Food allergy
Sicherer, S. H., & Sampson, H. A. (2006) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2005.05.048 · Cited by 647

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Background
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Embiriekah, S. M., Bulatović, M., Gnjatović, M., Vukašinović‐Sekulić, M., Krunić, T. Ž., Zarić, D. B., & Rakin, M. B. (2018) · Hemijska industrija · doi:10.2298/hemind171121019e · Cited by 4
“On the other hand, many food allergens are stable and resistant to digestion by gastrointestinal enzymes or are processed into high molecular weight peptides which retain the Immunoglobulin E (IgE) binding and T-cell-stimulating properties as it is the case of a bovine whey protein β-lactoglobulin [43,44].”
Background
Assessment of genetically modified maize DP910521 (application GMFF‐2021‐2473)
(GMO), E. P. O. G. M. O., Mullins, E., Bresson, J., Dalmay, T., Dewhurst, I. C., Epstein, M. M., Firbank, L. G., Guerche, P., Hejátko, J., Naegeli, H., et al. (2024) · EFSA Journal · doi:10.2903/j.efsa.2024.8887 · Cited by 4
“…that when characteristics of known food allergens are examined, one of the most prominent traits attributed to food allergens is protein stability (Breiteneder & Mills, 2005; Costa et al., 2022; Foo & Mueller, 2021; Helm, 2001). a. Effect of temperature and pH on NEPs The effects of temperature…”
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“High protein stability is required in allergen sensitization via the gastrointestinal tract because it is important to maintain proteolytic and hydrolytic resistance.(20) In developed countries, environmental pollution, changes in lifestyle and eating habits due to urbanization reveal contact with different allergens.”
Background
Brazil nut allergy: A review
Kluczkovski, A. M., & Vildes, M. S. (2015) · African Journal of Pharmacy and Pharmacology · doi:10.5897/ajpp2014.4206 · Cited by 3
“Protein versus Brazil nut allergy Since ingestion of some proteins is associated with allergic reactions in some consumers, Breiteneder and Mills (2005) summarized the common biochemical and physicochemical properties of food allergens.”
Background
Assessment of genetically modified maize DP4114 × MON 89034 × MON 87411 × DAS‐40278‐9 and subcombinations, for food and feed uses, under Regulation (EC) No 1829/2003 (application EFSA GMO‐NL‐2020‐171)
(GMO), E. P. O. G. M. O., Mullins, E. D., Bresson, J., Dalmay, T., Dewhurst, I. C., Epstein, M. M., Firbank, L. G., Guerche, P., Hejátko, J., Moreno, F. J., et al. (2022) · EFSA Journal · doi:10.2903/j.efsa.2022.7619 · Cited by 3
“It has been shown, for example, that when characteristics of known food allergens are examined, one prominent trait attributed to food allergens is protein stability (Helm, 2001; Breiteneder and Mills, 2005; Foo and Mueller, 2021; Costa et al., 2022).”
Assessment of genetically modified maize GA21 × T25 for food and feed uses, under Regulation (EC) No 1829/2003 (application EFSA‐GMO‐DE‐2016‐137)
(GMO), E. P. O. G. M. O., Mullins, E. D., Bresson, J., Dalmay, T., Dewhurst, I. C., Epstein, M. M., Firbank, L. G., Guerche, P., Hejátko, J., Moreno, F. J., et al. (2023) · EFSA Journal · doi:10.2903/j.efsa.2023.7729 · Cited by 3
“It has been shown, for example, that when characteristics of known food allergens are examined, one of the most prominent traits attributed to food allergens is protein stability (Helm, 2001; Breiteneder and Mills, 2005; Foo and Mueller, 2021; Costa et al., 2022).”
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Modeling of allergen proteins found in sea food products
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Self-citation
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“secalines from the group of prolamines [16].”
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“It has been shown that a prominent trait attributed to food allergens and protein safety is protein stability (Breiteneder & Mills, 2005; Costa et al., 2021; Foo & Müller, 2021; Helm, 2001).”
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“Across major allergen families, resistance to thermal denaturation and gastrointestinal proteolysis is a recurring feature of class I food allergens, which can sensitize via the gastrointestinal tract and are more frequently associated with systemic reactions [6,7].”
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Panel), E. P. O. G. M. O. (., Mullins, E. D., Bresson, J., Dalmay, T., Dewhurst, I. C., Epstein, M. M., Firbank, L. G., Guerche, P., Hejátko, J., Moreno, F. J., et al. (2023) · EFSA Journal · doi:10.2903/j.efsa.2023.8011 · Cited by 2
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Animal Models for Food Allergy
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Comparative Structural Proteomics of Allergenic Proteins from Plant Pollen
Salunke, D. M., Gill, J., & Dwevedi, A. (2014) · Journal of the Indian Institute of Science · Cited by 2
Informe del Comité Científico de la Agencia Española de Seguridad Alimentaria y Nutrición (AESAN) sobre alergias alimentarias
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Protecting Food‐Allergic Consumers: Managing Allergens across the Food Supply Chain
Kerbach, S., Alldrick, A. J., Crevel, R., Dömötör, L., DunnGalvin, A., Mills, E. N. C., Pfaff, S., Poms, R. E., Tömösközi, S., & Pöpping, B. (2010) · doi:10.1002/9780470644584.ch2 · Cited by 2
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“It has been shown that when characteristics of known food allergens are examined, a relevant trait attributed to food allergens is protein stability (Breiteneder & Mills, 2005; Costa et al., 2021; Foo & Müller, 2021; Helm, 2001).”
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Background
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“reflects an enhancement of atopy and allergic sensitization [14-16].”
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“Conversely, in seafood, there are two major groups of allergenic proteins: the tropomyosins of crustacean and mollusks and the calcium-binding parvalbumins present in fish and amphibians (Breiteneder and Mills, 2005).”
Background

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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