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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Yap, P., & Gan, C. (2020) · Trends in Food Science & Technology · doi:10.1016/j.tifs.2020.09.005 · Cited by 54
Hypoallergenic Legume Crops and Food Allergy: Factors Affecting Feasibility and Risk
Riascos, J. J., Weissinger, A. K., Weissinger, S. M., & Burks, A. W. (2009) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf902526y · Cited by 53
Identification of a New Natural Ara h 6 Isoform and of Its Proteolytic Product as Major Allergens in Peanut
Bernard, H., Mondoulet, L., Drumare, M. ‐., Paty, E., Scheinmann, P., Thaï, R., & Wal, J. M. (2007) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf071424g · Cited by 50
Innate immunostimulatory properties of allergens and their relevance to food allergy
Ruiter, B., & Shreffler, W. G. (2012) · Seminars in Immunopathology · doi:10.1007/s00281-012-0334-8 · Cited by 47
“A very common feature of both food and respiratory allergens, including many prolamins (non-specific lipid transfer proteins, 2S albumins, prolamin storage proteins and α-amylase/trypsin inhibitors) as well as lipocalins and some cupins, is lipid binding [16, 17].”
Characterization of potential allergens in fenugreek (Trigonella foenum-graecum) using patient sera and MS-based proteomic analysis
Fæste, C. K., Christians, U., Egaas, E., & Jonscher, K. R. (2010) · Journal of Proteomics · doi:10.1016/j.jprot.2010.02.011 · Cited by 47
“The rising prevalence [8] and seriousness of peanut allergy [9] has led to a corresponding increase in studies evaluating the allergenic potentials of the individual peanut proteins, including members of four dominant plant allergen families [10,11].”
Background
The lipid interaction capacity of Sin a 2 and Ara h 1, major mustard and peanut allergens of the cupin superfamily, endorses allergenicity
Angelina, A., Sirvent, S., Palladino, C., Vereda, A., Cuesta‐Herranz, J., Eiwegger, T., Rodrı́guez, R., Breiteneder, H., Villalba, M., & Palomares, Ó. (2016) · Allergy · doi:10.1111/all.12887 · Cited by 47
“Food allergens that are able to sensitize via the gastrointestinal tract share common features such as relatively low molecular weight (10–70 kDa), high solubility in biologic fluids, thermal stability, and digestion resistance (17, 18).”
BackgroundSelf-citation
Mass spectrometric analysis of allergens in roasted walnuts
Downs, M. L., Baumert, J. L., Taylor, S. L., & Mills, E. N. C. (2016) · Journal of Proteomics · doi:10.1016/j.jprot.2016.04.045 · Cited by 47
Self-citation
Pistachio nut allergy: An updated overview
Costa, J. S., Silva, I., Vicente, A. A., Oliveira, M. B. P. P., & Mafra, I. (2017) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2017.1379947 · Cited by 47
The Seed Biotinylated Protein of Soybean (Glycine max): A Boiling-Resistant New Allergen (Gly m 7) with the Capacity To Induce IgE-Mediated Allergic Responses
Riascos, J. J., Weissinger, S. M., Weissinger, A. K., Kulis, M. D., Burks, A. W., & Pons, L. (2016) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.5b05873 · Cited by 46
A robust method for the estimation and visualization of IgE cross-reactivity likelihood between allergens belonging to the same protein family
Chruszcz, M., Kapingidza, A. B., Dolamore, C., & Kowal, K. (2018) · PLoS ONE · doi:10.1371/journal.pone.0208276 · Cited by 48
Allergenicity of Proteolytic Hydrolysates of the Soybean 11S Globulin
Lee, H. ‐., Eunyoung, K. E. U. M., Lee, S., Sung, D.-E., Chung, D. ‐., Lee, S., & Oh, S. (2007) · Journal of Food Science · doi:10.1111/j.1750-3841.2007.00307.x · Cited by 46
Food allergy: When mucosal immunity goes wrong
Sampson, H. A. (2005) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2004.11.003 · Cited by 46
Unfolded phosphopolypeptides enable soft and hard tissues to coexist in the same organism with relative ease
Holt, C. (2013) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2013.02.010 · Cited by 46
Effect of simulated gastro‐duodenal digestion on the allergenic reactivity of beta‐lactoglobulin
Bossios, A., Theodoropoulou, M., Mondoulet, L., Rigby, N. M., Papadopoulos, N. G., Bernard, H., Adel‐Patient, K., Wal, J. M., Mills, E. N. C., & Papageorgiou, P. S. (2011) · Clinical and Translational Allergy · doi:10.1186/2045-7022-1-6 · Cited by 46
“The mechanism underlying the protective effect of PC on blg breakdown in the duodenal environment is not clear but may relate to the ability of blg to bind lipids, ligand binding stabilising proteins [10] or interactions of a subtle nature with lipids as have been found to play a role in the protective effect of PC on…”
BackgroundSelf-citation
Should digestion assays be used to estimate persistence of potential allergens in tests for safety of novel food proteins?
Schnell, S. D., & Herman, R. A. (2009) · Clinical and Molecular Allergy · doi:10.1186/1476-7961-7-1 · Cited by 45
“Typical diets contain tens of thousands of different proteins, and efforts to understand the unique physiochemical and molecular properties of food allergens are ongoing [13-15].”
Background
Structural analysis of linear and conformational epitopes of allergens
Ivanciuc, O., Schein, C. H., Garcia, T., Oezguen, N., Negi, S. S., & Braun, W. A. (2008) · Regulatory Toxicology and Pharmacology · doi:10.1016/j.yrtph.2008.11.007 · Cited by 45
“…clinically important cross-reactivities among environmental triggers of allergy and asthma can be accounted for by proteins in those sources that have common molecular properties (Breiteneder and Ebner, 2000; Mari, 2001; Ferreira et al., 2004; Breiteneder and Mills, 2005; Jenkins et al., 2005).”
Background
Ligand binding to an Allergenic Lipid Transfer Protein Enhances Conformational Flexibility resulting in an Increase in Susceptibility to Gastroduodenal Proteolysis
Abdullah, S. U., Alexeev, Y., Johnson, P. E., Rigby, N. M., Mackie, A. R., Dhaliwal, B., & Mills, E. N. C. (2016) · Scientific Reports · doi:10.1038/srep30279 · Cited by 44
Self-citation
Immunological behavior of in vitro digested egg-white lysozyme.
Jiménez-Saiz, R., Benedé, S., Miralles, B., López-Expósito, I., Molina, E., & López-Fandiño, R. (2014) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201300442 · Cited by 40
Immunoglobulin E cross-reactivity between lupine conglutins and peanut allergens in serum of lupine-allergic individuals.
Dooper, M. M. B. W., Plassen, C., Holden, L., Lindvik, H., & Fæste, C. K. (2009) · PubMed · Cited by 44
Insoluble and soluble roasted walnut proteins retain antibody reactivity.
Downs, M., Simpson, A., Čustović, A., Semic-Jusufagic, A., Bartra, J., Fernández-Rivas, M., Taylor, S., Baumert, J., & Mills, E. N. C. (2016) · Food Chemistry · doi:10.1016/j.foodchem.2015.08.119 · Cited by 39
Self-citation
Structural Stability of Amandin, a Major Allergen from Almond (Prunus dulcis), and Its Acidic and Basic Polypeptides
Albillos, S. M., Menhart, N., & Fu, T. (2009) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf803977z · Cited by 43
Effect of Heat Treatment on the Detection of Intact Bovine β-Lactoglobulins by LC Mass Spectrometry
Monaci, L., & van Hengel, A. J. (2007) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf063083x · Cited by 42
Common Physical−Chemical Properties Correlate with Similar Structure of the IgE Epitopes of Peanut Allergens
Schein, C. H., Ivanciuc, O., & Braun, W. A. (2005) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf051148a · Cited by 42
Digestibility and antigenicity of β-lactoglobulin as affected by heat, pH and applied shear
Rahaman, T., Vasiljevic, T., & Ramchandran, L. (2016) · Food Chemistry · doi:10.1016/j.foodchem.2016.08.129 · Cited by 42
“S bonds (Breiteneder & Mills, 2005).”
Combined microwave processing and enzymatic proteolysis of bovine whey proteins: the impact on bovine β-lactoglobulin allergenicity
Mecherfi, K. E. E., Curet, S., Lupi, R., Larré, C., Rouaud, O., Choiset, Y., Rabesona, H., & Haertlé, T. (2018) · Journal of Food Science and Technology · doi:10.1007/s13197-018-3471-9 · Cited by 42
Influence of plant lipids on immune responses in mice to the major Brazil nut allergen Ber e 1
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Proteomics-based allergen analysis in plants
Nakamura, R., & Teshima, R. (2013) · Journal of Proteomics · doi:10.1016/j.jprot.2013.03.018 · Cited by 41
Bioinformatic screening and detection of allergen cross‐reactive IgE‐binding epitopes
McClain, S. (2017) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201600676 · Cited by 41
“Only Ara h 1 and two beta-conglycinin proteins from soybean showed alignments, both vicilin-like 7S globulins [25, 26]; the least significant alignment was 2.”
Background
Food allergy in gastroenterologic diseases: Review of literature
Mansueto, P. (2006) · World Journal of Gastroenterology · doi:10.3748/wjg.v12.i48.7744 · Cited by 41

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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Molecular properties of food allergens

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