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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Carbohydrate chains normally exert a stabilizing effect on protein structure, offering protection towards processing and/or gastroduodenal digestion and thus contributing to allergenic potential.
“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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A classification of plant food allergens*1
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Self-citationPartial Purification and Characterization of the 15S Globulin of Soybeans, a Dimer of Glycinin
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Intrinsic properties of allergens and environmental exposure as determinants of allergenicity*
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The molecular basis for N-glycosylation in the 11S globulin (legumin) of lupin seed
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Purification and characterization of an allergen of mustard seed.
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Epitope Mapping Studies of Broad Specificity Monoclonal Antibodies to Cereal Prolamins
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Genetic origin of diversity of human cytoskeletal tropomyosins
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The EF-Hand Calcium-Binding Proteins
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Transproteomic evidence of loop-deletion mechanism for enhancing protein thermostability
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Interaction of Surfactants and Polymer-Grafted Lipids with a Plant Lipid Transfer Protein, LTP1
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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 · see citing works
Self-citationSicherer, S. H., & Sampson, H. A. (2006) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2005.05.048 · Cited by 647 · see citing works
Panel), E. P. O. G. M. O. (. (2010) · EFSA Journal · doi:10.2903/j.efsa.2010.1700 · Cited by 610 · see citing works
Nonmeat Protein Alternatives as Meat Extenders and Meat Analogs
Asgar, M. A., Fazilah, A., Huda, N., Bhat, R., & Karim, A. A. (2010) · Comprehensive Reviews in Food Science and Food Safety · doi:10.1111/j.1541-4337.2010.00124.x · Cited by 505 · see citing works
Radauer, C., Bublin, M., Wagner, S., Mari, A., & Breiteneder, H. (2008) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2008.01.025 · Cited by 477 · see citing works
“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,…”
BackgroundSelf-citationValenta, R., Hochwallner, H., Linhart, B., & Pahr, S. (2015) · Gastroenterology · doi:10.1053/j.gastro.2015.02.006 · Cited by 298 · see citing works
EAACI Molecular Allergology User's Guide 2.0
Dramburg, S., Hilger, C., Santos, A. F., Vecillas, L. D. L., Aalberse, R. C., Acevedo, N., Aglas, L., Altmann, F., Arruda, L. K., Asero, R., et al. (2023) · Pediatric Allergy and Immunology · doi:10.1111/pai.13854 · Cited by 332 · see citing works
Self-citationRole of plant lipid transfer proteins in plant cell physiology—A concise review
Carvalho, A. D. O., & Gomes, V. M. (2007) · Peptides · doi:10.1016/j.peptides.2007.03.004 · Cited by 278 · see citing works
Ekezie, F.-G. C., Cheng, J., & Sun, D. (2018) · Trends in Food Science & Technology · doi:10.1016/j.tifs.2018.01.007 · Cited by 269 · see citing works
Rare, medium, or well done? The effect of heating and food matrix on food protein allergenicity
Nowak-Wegrzyn, A. H., & Fiocchi, A. G. (2009) · Current Opinion in Allergy and Clinical Immunology · doi:10.1097/aci.0b013e32832b88e7 · Cited by 263 · see citing works
Milk allergens, their characteristics and their detection in food: A review
Monaci, L., Trégoat, V., van Hengel, A. J., & Anklam, E. (2006) · European Food Research and Technology · doi:10.1007/s00217-005-0178-8 · Cited by 259 · see citing works
Evolutionary biology of plant food allergens
Radauer, C., & Breiteneder, H. (2007) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2007.07.024 · Cited by 255 · see citing works
Self-citationScientific Opinion on the evaluation of allergenic foods and food ingredients for labelling purposes
EFSA Panel on Dietetic Products, N. A. A. (. (2014) · EFSA Journal · doi:10.2903/j.efsa.2014.3894 · Cited by 243 · see citing works
Roth-Walter, F., Berin, M., Arnaboldi, P., Escalante, C., Dahan, S., Rauch, J., Jensen-Jarolim, E., & Mayer, L. F. (2008) · Allergy. European Journal of Allergy and Clinical Immunology · doi:10.1111/j.1398-9995.2008.01673.x · Cited by 215 · see citing works
“It is to note that, so far, all known major food allergens tend to form pseudo-lipophilic protein-bodies (30), micelles (31, 32) or aggregates (6) and consequently their ability to enter the body through absorptive intestinal epithelial cells is predicted to be diminished.”
BackgroundGastrointestinal digestion of food allergens: Effect on their allergenicity
Moreno, F. J. (2006) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2006.10.005 · Cited by 221 · see citing works
Fish Allergens at a Glance: Variable Allergenicity of Parvalbumins, the Major Fish Allergens
Kuehn, A., Swoboda, I., Arumugam, K., Hilger, C., & Hentges, F. (2014) · Frontiers in Immunology · doi:10.3389/fimmu.2014.00179 · Cited by 203 · see citing works
“The structural stability has been allocated to different protein characteristics such as intrinsic ligand binding and intramolecular disulfide bonds (41).”
Transforming insect biomass into consumer wellness foods: A review
Sun‐Waterhouse, D., Waterhouse, G. I. N., You, L., Zhang, J., Liu, Y., Ma, L., Gao, J., & Dong, Y. (2016) · Food Research International · doi:10.1016/j.foodres.2016.10.001 · Cited by 188 · see citing works
“…higher thermal stability, resistance to proteolysis, binding capacity and interactive potential with lipids and/or ions like Cu2+ (especially high stability under the acidic and proteolytic conditions in the digestive tract), typically exhibit greater allergenicity (Breiteneder and Mills, 2005).”
BackgroundDong, X., Wang, J., & Raghavan, V. (2020) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2020.1722942 · Cited by 188 · see citing works
Are Physicochemical Properties Shaping the Allergenic Potency of Plant Allergens?
Costa, J. S., Bavaro, S. L., Benedé, S., Díaz‐Perales, A., Bueno, C., Gelencsér, É., Klueber, J., Larré, C., Lozano‐Ojalvo, D., Lupi, R., et al. (2020) · Clinical Reviews in Allergy & Immunology · doi:10.1007/s12016-020-08810-9 · Cited by 181 · see citing works
Akdiş, C. A. (2006) · Current Opinion in Immunology · doi:10.1016/j.coi.2006.09.016 · Cited by 175 · see citing works
Impairing oral tolerance promotes allergy and anaphylaxis: A new murine food allergy model
Ganeshan, K., Neilsen, C. V., Hadsaitong, A., Schleimer, R. P., Luo, X., & Bryce, P. J. (2008) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2008.10.011 · Cited by 169 · see citing works
“Most allergens in food share similar chemical properties (ie, heat, acid, and enzymatic stability).(11) Food allergens are considerably more stable in simulated gastric fluid than nonantigenic proteins,(12) and reducing protein breakdown by acid neutralization increased antigen immunogenicity in mice.”
Mandalari, G., Adel‐Patient, K., Barkholt, V., Baro, C., Bennett, L., Bublin, M., Gaier, S. A., Graser, G., Ladics, G. S., Mierzejewska, D., et al. (2009) · Regulatory Toxicology and Pharmacology · doi:10.1016/j.yrtph.2009.08.010 · Cited by 167 · see citing works
Self-citationPlant food allergens—structural and functional aspects of allergenicity
Breiteneder, H., & Mills, E. N. C. (2005) · Biotechnology Advances · doi:10.1016/j.biotechadv.2005.05.004 · Cited by 155 · see citing works
Self-citationPekar, J., Ret, D., & Untersmayr, E. (2018) · Molecular Immunology · doi:10.1016/j.molimm.2018.03.017 · Cited by 141 · see citing works
Mechanisms of peripheral tolerance to allergens
Soyer, O. U., Akdiş, M., Ring, J., Behrendt, H., Crameri, R., Lauener, R. P., & Akdiş, C. A. (2012) · Allergy · doi:10.1111/all.12085 · Cited by 131 · see citing works
“A high number of disulfide bonds and occasionally disordered structures designed for protein stability and mobility have been observed (4).”
BackgroundMechanisms underlying differential food allergy response to heated egg
Martos, G., Lopez-Exposito, I., Bencharitiwong, R., Berin, M. C., & Nowak-Węgrzyn, A. (2011) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2011.01.057 · Cited by 145 · see citing works
Moreno, F. J., Mackie, A. R., & Mills, E. N. C. (2005) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf0515227 · Cited by 128 · see citing works
Self-citationLipid transfer protein allergy: primary food allergy or pollen/food syndrome in some cases
Zuidmeer, L., & van Ree, R. (2007) · Current Opinion in Allergy and Clinical Immunology · doi:10.1097/aci.0b013e32814a5401 · Cited by 116 · see citing works
Effect of high-pressure treatment on in-vitro digestibility of β-lactoglobulin
Zeece, M. G., Huppertz, T., & Kelly, A. L. (2007) · Innovative Food Science & Emerging Technologies · doi:10.1016/j.ifset.2007.05.004 · Cited by 115 · see citing works
Vissers, Y. M., Iwan, M., Adel‐Patient, K., Skov, P. S., Rigby, N. M., Johnson, P. E., Müller, P. M., Przybylski‐Nicaise, L., Schaap, M., Ruinemans‐Koerts, J., et al. (2011) · Clinical & Experimental Allergy · doi:10.1111/j.1365-2222.2011.03830.x · Cited by 115 · see citing works
Self-citationPeanut Composition, Flavor and Nutrition
Davis, J. P., & Dean, L. L. (2016) · Elsevier eBooks · doi:10.1016/b978-1-63067-038-2.00011-3 · Cited by 108 · see citing works
Bioinformatics Approaches to Classifying Allergens and Predicting Cross-Reactivity
Schein, C. H., Ivanciuc, O., & Braun, W. A. (2007) · Immunology and Allergy Clinics of North America · doi:10.1016/j.iac.2006.11.005 · Cited by 99 · see citing works
“These successes explain the current interest in developing bioinformatics approaches to interpret the accumulated body of knowledge about the proteins that elicit severe IgE-mediated reactions [8,68–70].”
BackgroundProtein Digestion of Baby Foods: Study Approaches and Implications for Infant Health
Gan, J., Bornhorst, G. M., Henrick, B. M., & German, J. B. (2017) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201700231 · Cited by 96 · see citing works
“Resistance to digestion is a characteristic of food allergens [21].”
BackgroundThe frontiers of mass spectrometry-based techniques in food allergenomics
Picariello, G., Mamone, G., Addeo, F., & Ferranti, P. (2011) · Journal of Chromatography A · doi:10.1016/j.chroma.2011.06.033 · Cited by 95 · see citing works
Food Allergy Overview in Children
Ramesh, S. (2007) · Clinical Reviews in Allergy & Immunology · doi:10.1007/s12016-007-8034-1 · Cited by 94 · see citing works
“Other pathogenesisrelated proteins such as Thaumatin-like proteins are also involved [72].”
BackgroundIgE-binding epitopes: a reappraisal
Aalberse, R. C., & Crameri, R. (2011) · Allergy · doi:10.1111/j.1398-9995.2011.02656.x · Cited by 93 · see citing works
“Intra-individual differences between the IgE and IgG(4) allergen epitope repertoire It is often implicitly assumed that the spectrum of allergenderived IgE epitopes does not fully overlap with that of epitopes recognized by other isotypes.”
BackgroundInfluentialEiwegger, T., Rigby, N. M., Mondoulet, L., Bernard, H., Krauth, M. T., Boehm, A., Dehlink, E., Valent, P., Wal, J. M., Mills, E. N. C., et al. (2006) · Clinical & Experimental Allergy · doi:10.1111/j.1365-2222.2006.02565.x · Cited by 93 · see citing works
Self-citationMills, E. N. C., Jenkins, J. A., & Shewry, P. R. (2006) · Plant Biotechnology · doi:10.1002/0470021837.ch13 · Cited by 89 · see citing works
Self-citationVassilopoulou, Ε., Rigby, N. M., Moreno, F. J., Zuidmeer, L., Akkerdaas, J. H., Tassios, I., Papadopoulos, N. G., Saxoni‐Papageorgiou, P., van Ree, R., & Mills, E. N. C. (2006) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2006.04.057 · Cited by 88 · see citing works
Self-citationCunsolo, V., Saletti, R., Muccilli, V., Gallina, S., Francesco, A. D., & Foti, S. (2017) · Food Research International · doi:10.1016/j.foodres.2017.07.002 · Cited by 88 · see citing works
Sathe, S. K., Liu, C., & Zaffran, V. D. (2016) · Annual Review of Food Science and Technology · doi:10.1146/annurev-food-041715-033308 · Cited by 88 · see citing works
Dreskin, S. C., Koppelman, S. J., Andorf, S., Nadeau, K. C., Kalra, A., Braun, W. A., Negi, S. S., Chen, X., & Schein, C. H. (2020) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2020.11.004 · Cited by 86 · see citing works
Stanić-Vučinić, D., Stojadinović, M., Atanasković‐Marković, M., Ognjenović, J., Grönlund, H., van Hage, M., Lantto, R., Sancho, A. I., & Veličković, T. Ć. (2012) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201200179 · Cited by 85 · see citing works
“In solution, due to its very compact fold, BLG is highly stable to denaturation and resistant to proteolytic hydrolysis [18].”
BackgroundLi, T., Bu, G., & Xi, G. (2020) · Food Chemistry · doi:10.1016/j.foodchem.2020.128962 · Cited by 82 · see citing works
TH2 adjuvants: Implications for food allergy
Berin, M. C., & Shreffler, W. G. (2008) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2008.04.023 · Cited by 81 · see citing works
Egg proteins as allergens and the effects of the food matrix and processing.
Benedé, S., López-Expósito, I., Molina, E., & López-Fandiño, R. (2015) · Food & Function · doi:10.1039/c4fo01104j · Cited by 75 · see citing works
Redefining the major peanut allergens
Zhuang, Y., & Dreskin, S. C. (2012) · Immunologic Research · doi:10.1007/s12026-012-8355-x · Cited by 80 · see citing works
Cui, J., Han, L., Li, H., Ung, C. Y., Tang, Z. Q., Zheng, C., Cao, Z. W., & Chen, Y. (2006) · Molecular Immunology · doi:10.1016/j.molimm.2006.02.010 · Cited by 78 · see citing works
From pollinosis to digestive allergy.
Bartra, J., Sastre, J., del Cuvillo, A., Montoro, J., Jauregui, I., Davila, I. J., Ferrer, M., Mullol, J., & Valero, A. (2009) · PubMed · Cited by 74 · see citing works
Monaci, L., Brohée, M., Trégoat, V., & van Hengel, A. J. (2011) · Food Chemistry · doi:10.1016/j.foodchem.2010.12.113 · Cited by 72 · see citing works
Adsorption and Structural Change of β-Lactoglobulin at the Diacylglycerol−Water Interface
Sakuno, M. M., Matsumoto, S., Kawai, S., Koseki, T., & Matsumura, Y. (2008) · Langmuir · doi:10.1021/la8018277 · Cited by 71 · see citing works
Zhang, Y., Wu, Z., Li, K., Li, X., Yang, A., Tong, P., & Chen, H. (2018) · Food Chemistry · doi:10.1016/j.foodchem.2018.12.070 · Cited by 70 · see citing works
Enzymatic crosslinking and food allergenicity: A comprehensive review
Ahmed, I., Chen, H., Li, J., Wang, B., Li, Z., & Huang, G. (2021) · Comprehensive Reviews in Food Science and Food Safety · doi:10.1111/1541-4337.12855 · Cited by 69 · see citing works
Digested Ara h 1 has sensitizing capacity in Brown Norway rats
Bøgh, K. L., Kroghsbo, S., Dahl, L., Rigby, N. M., Barkholt, V., Mills, E. N. C., & Madsen, C. B. (2009) · Clinical & Experimental Allergy · doi:10.1111/j.1365-2222.2009.03333.x · Cited by 69 · see citing works
Self-citationScossa, F., Laudencia‐Chingcuanco, D., Anderson, O. D., Vensel, W. H., Lafiandra, D., D'Ovidio, R., & Masci, S. (2008) · PROTEOMICS · doi:10.1002/pmic.200700861 · Cited by 68 · see citing works
“, celiac disease), wheat grains contain a high concentration of potentially allergenic polypeptides [66] that mostly belong to this fraction.”
Background(GMO), E. P. O. G. M. O., Naegeli, H., Bresson, J., Dalmay, T., Dewhurst, I. C., Epstein, M. M., Firbank, L. G., Guerche, P., Hejátko, J., Moreno, F. J., et al. (2021) · EFSA Journal · doi:10.2903/j.efsa.2021.6350 · Cited by 65 · see citing works
“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; Costa et al., 2021).”
BackgroundEvaluation and integration of existing methods for computational prediction of allergens
Wang, J., Yu, Y., Zhao, Y., Zhang, D., & Li, J. (2013) · BMC Bioinformatics · doi:10.1186/1471-2105-14-s4-s1 · Cited by 65 · see citing works
“Since allergenic proteins were reported have specific physiological functions and highly similar folding structures [31-34], taking the protein families classification and folding or 3D structures into the allergen prediction would be helpful to solve this issue.”
BackgroundNonspecific lipid-transfer proteins in plant foods and pollens: an important allergen class
Breiteneder, H., & Mills, E. N. C. (2005) · Current Opinion in Allergy and Clinical Immunology · doi:10.1097/01.all.0000168794.35571.a5 · Cited by 64 · see citing works
Self-citationPérez, O. E., David-Birman, T., Kesselman, E., Levi-Tal, S., & Lesmes, U. (2013) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2013.11.010 · Cited by 62 · see citing works
Epitope characterization of ovalbumin in BALB/c mice using different entry routes
Mine, Y., & Yang, M. (2006) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2006.12.003 · Cited by 62 · see citing works
Oberhuber, C., Bulley, S. M., Ballmer-Weber, B. K., Bublin, M., Gaier, S., DeWitt, Å. M., Briza, P., Hofstetter, G., Lidholm, J., Vieths, S., et al. (2008) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.200800146 · Cited by 62 · see citing works
“These findings can be explained by heat lability and low resistance to digestion of the Bet v 1 homologous proteins [30].”
BackgroundMecherfi, K. E. E., Saïdi, D., Khéroua, O., Boudraa, G., Touhami, M., Rouaud, O., Curet, S., Choiset, Y., Rabesona, H., Chobert, J., et al. (2011) · European Food Research and Technology · doi:10.1007/s00217-011-1581-y · Cited by 62 · see citing works
“b-Lg is mainly used for its functional uses in food systems; however, it is also a major allergen [27–29].”
BackgroundMasilamani, M., Commins, S., & Shreffler, W. (2012) · Immunology and allergy clinics of North America · doi:10.1016/j.iac.2011.12.003 · Cited by 58 · see citing works
Brambilla, F., Resta, D., Isak, I., Zanotti, M., & Arnoldi, A. (2008) · PROTEOMICS · doi:10.1002/pmic.200800317 · Cited by 60 · see citing works
Linking iron-deficiency with allergy: role of molecular allergens and the microbiome
Roth‐Walter, F., Pacios, L. F., Bianchini, R., & Jensen‐Jarolim, E. (2017) · Metallomics · doi:10.1039/c7mt00241f · Cited by 61 · see citing works
“103 All members of these families share certain characteristics like their great structural stability and their ability to serve as carriers for a variety of compounds with lipidic segments.”
BackgroundMoreno, F. J., Rubio, L. A., Olano, A., & Clemente, A. (2006) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf061760h · Cited by 59 · see citing works
Characterization of lupin major allergens (Lupinus albus L.)
Guillamón, E., Rodríguez, J., Burbano, C., Múzquiz, M., Pedrosa, M. M., Cabanillas, B., Crespo, J. F., Sancho, A. I., Mills, E. N. C., & Cuadrado, C. (2010) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.200900452 · Cited by 59 · see citing works
“The presence of disulphide bonds in a protein is one of the structural characteristics involved in conferring heat stability, together with the cupin barrel itself [44].”
BackgroundSelf-citationHigh pressure effects on allergen food proteins
Somkuti, J., & Smeller, L. (2013) · Biophysical Chemistry · doi:10.1016/j.bpc.2013.06.009 · Cited by 57 · see citing works
Ciarmiello, L. F., Mazzeo, M. F., Minasi, P., Peluso, A., Luca, A. D., Piccirillo, P., Siciliano, R. A., & Carbone, V. (2014) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf5018324 · Cited by 57 · see citing works
An overview on fish and shellfish allergens and current methods of detection
Fernandes, T. J. R., Costa, J. S., Oliveira, M. B. P. P., & Mafra, I. (2015) · Food and Agricultural Immunology · doi:10.1080/09540105.2015.1039497 · Cited by 55 · see citing works
“Tropomyosins are present in muscle and non-muscle cells, and together with actin and myosin, they intervene in the regulatory process of muscle contraction (Breiteneder & Mills, 2005; Leung et al., 2014).”
BackgroundMolecular Properties of Plant Food Allergens: A Current Classification into Protein Families
Ferreira, F., Hauser, M., Egger, M., Wallner, M., Wopfner, N., & Schmidt, G. (2008) · The Open Immunology Journal · doi:10.2174/1874226200801010001 · Cited by 54 · see citing works
“However, severe forms of PFS including anaphylaxis have been attributed to the Bet v 1 homologue Gly m 4 from soybean [1, 12].”
BackgroundYap, P., & Gan, C. (2020) · Trends in Food Science & Technology · doi:10.1016/j.tifs.2020.09.005 · Cited by 54 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
“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].”
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 · see citing works
“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].”
BackgroundAngelina, 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 · see citing works
“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-citationMass 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 · see citing works
Self-citationPistachio 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 · see citing works
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 · see citing works
Chruszcz, M., Kapingidza, A. B., Dolamore, C., & Kowal, K. (2018) · PLoS ONE · doi:10.1371/journal.pone.0208276 · Cited by 48 · see citing works
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 · see citing works
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 · see citing works
Holt, C. (2013) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2013.02.010 · Cited by 46 · see citing works
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 · see citing works
“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…”
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“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].”
BackgroundStructural 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 · see citing works
“…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).”
BackgroundAbdullah, 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 · see citing works
Self-citationImmunological 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 · see citing works
Dooper, M. M. B. W., Plassen, C., Holden, L., Lindvik, H., & Fæste, C. K. (2009) · PubMed · Cited by 44 · see citing works
Insoluble and soluble roasted walnut proteins retain antibody reactivity
Downs, M. L., Simpson, A., Čustović, A., Semic‐Jusufagic, A., Bartra, J., Fernández‐Rivas, M., Taylor, S. L., Baumert, J. L., & Mills, E. N. C. (2015) · Food Chemistry · doi:10.1016/j.foodchem.2015.08.119 · Cited by 43 · see citing works
Self-citationAlbillos, S. M., Menhart, N., & Fu, T. (2009) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf803977z · Cited by 43 · see citing works
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 · see citing works
Schein, C. H., Ivanciuc, O., & Braun, W. A. (2005) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf051148a · Cited by 42 · see citing works
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 · see citing works
“S bonds (Breiteneder & Mills, 2005).”
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 · see citing works
Influence of plant lipids on immune responses in mice to the major Brazil nut allergen Ber e 1
Dearman, R. J., Alcocer, M. J. C., & Kimber, I. (2007) · Clinical & Experimental Allergy · doi:10.1111/j.1365-2222.2007.02689.x · Cited by 42 · see citing works
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 · see citing works
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 · see citing works
“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.”
BackgroundFood allergy in gastroenterologic diseases: Review of literature
Mansueto, P. (2006) · World Journal of Gastroenterology · doi:10.3748/wjg.v12.i48.7744 · Cited by 41 · see citing works
- 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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