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

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

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

DOI 10.1016/j.jaci.2004.10.022

Open this paper in CoChat — free account

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.

Integrity signals

Registry

Crossref · 10.1016/j.jaci.2004.10.022

Cites

119 of 119 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

We couldn’t retrieve this paper’s full text, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Food Allergy
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

Flagged first, then by citations

Show all 119 references

Sorted by citations

Items 101–200 of 359

Differential immunogenicity and allergenicity of native and recombinant human lactoferrins: Role of glycosylation
Almond, R., Flanagan, B., Antonopoulos, A., Haslam, S., Dell, A., Kimber, I., & Dearman, R. (2013) · European Journal of Immunology · doi:10.1002/eji.201142345 · Cited by 43
Responsiveness of the major birch allergen Bet v 1 scaffold to the gastric environment: Impact on structure and allergenic activity
Sancho, A. I., Wangorsch, A., Jensen, B. M., Watson, A., Alexeev, Y., Johnson, P. E., Mackie, A. R., Neubauer, A., Reese, G., Ballmer-Weber, B. K., et al. (2011) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201100025 · Cited by 40
“This might be explained by the apparent lability of these proteins following pepsin digestion [8] with an associated loss of IgE reactivity, although the resulting peptides are still able to activate pollen-specific T cells [9].”
BackgroundInfluential
Plant Food Allergies: A Suggested Approach to Allergen-Resolved Diagnosis in the Clinical Practice by Identifying Easily Available Sensitization Markers
Asero, R. (2005) · International Archives of Allergy and Immunology · doi:10.1159/000087352 · Cited by 40
“induces in vitro basophil histamine release and has the potential to elicit allergic reactions in vivo. However, in both cases, the allergen concentrations needed to achieve mediator release were relatively high [”
Characterization of plant food allergens: An overview on physicochemical and immunological techniques
Harrer, A., Egger, M., Gadermaier, G., Erler, A., Hauser, M., Ferreira, F., & Himly, M. (2009) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.200900096 · Cited by 39
Heating Affects Structure, Enterocyte Adsorption and Signalling, As Well as Immunogenicity of the Peanut Allergen Ara h 2
Starkl, P. M., Krishnamurthy, D., Szalai, K., Felix, F., Lukschal, A., Oberthüer, D., Sampson, H. A., Swoboda, I., Betzel, C., Untersmayr, E., et al. (2011) · The Open Allergy Journal · doi:10.2174/1874838401104010024 · Cited by 38
“In addition to genetic predisposition, environmental factors and structural features of allergenic proteins are of major importance [5, 29, 30].”
Molecular fragmentation of wheat-germ agglutinin induced by food irradiation reduces its allergenicity in sensitised mice
Vaz, A. F. D. M., de Souza, M. P., Carneiro‐da‐Cunha, M. G., de Medeiros, P. L., Melo, A. M. M. D. A., Aguiar, J. D. S., da Silva, T. G., Silva-Lucca, R. A., Oliva, M. L. V., & Correia, M. T. D. S. (2011) · Food Chemistry · doi:10.1016/j.foodchem.2011.11.097 · Cited by 38
An attempt to define allergen-specific molecular surface features: a bioinformatic approach
Furmonaviciene, R., Sutton, B. J., Glaser, F., Laughton, C. A., Jones, N., Sewell, H. F., & Shakib, F. (2005) · Bioinformatics · doi:10.1093/bioinformatics/bti700 · Cited by 38
“Examples of such ligands include metal ions (e.g. Ca in parvalbumins) and lipids (e.g. MD-2 proteins, lipocalins and lipid transfer proteins) (Breiteneder and Mills, 2005).”
Novel Polyclonal−Monoclonal-Based ELISA Utilized To Examine Lupine (Lupinus Species) Content in Food Products
Holden, L., Moen, L. H., Sletten, G. B. G., & Dooper, M. M. B. W. (2007) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf063320w · Cited by 37
Characterization of physicochemical and immunogenic properties of allergenic proteins altered by food processing: a review
Zhou, E., Li, Q., Zhu, D., Chen, G., & Wu, L. (2023) · Food Science and Human Wellness · doi:10.26599/fshw.2022.9250095 · Cited by 39
Assessment of the Sensitizing Potential of Processed Peanut Proteins in Brown Norway Rats: Roasting Does Not Enhance Allergenicity
Kroghsbo, S., Rigby, N. M., Johnson, P. E., Adel‐Patient, K., Bøgh, K. L., Salt, L. J., Mills, E. N. C., & Madsen, C. B. (2014) · PLoS ONE · doi:10.1371/journal.pone.0096475 · Cited by 36
“Certainly, both food processing and structure of the food matrix may impact allergenicity of food allergens [1–4].”
BackgroundSelf-citation
Assessment of the potential allergenicity of genetically-engineered food crops
Ladics, G. (2018) · Journal of Immunotoxicology · doi:10.1080/1547691x.2018.1533904 · Cited by 24
“Several protein allergens are glycosylated, implying the possibility that the glycosyl groups may contribute to their allergenicity (Huby et al. 2000; Breiteneder and Mills 2005).”
Background
Impact of lipid binding on the tertiary structure and allergenic potential of Jug r 3, the non-specific lipid transfer protein from walnut
Dubiela, P., Conte, R. D., Cantini, F., Borowski, T., Aina, R., Radauer, C., Bublin, M., Hoffmann‐Sommergruber, K., & Alessandri, S. (2019) · Scientific Reports · doi:10.1038/s41598-019-38563-1 · Cited by 37
Effects of high hydrostatic pressure treatment on the antigenicity, structural and digestive properties of whey protein
Jiang, H., Zhang, Z., Wang, Y., Gao, J., Yuan, Q., & Mao, X. (2023) · LWT · doi:10.1016/j.lwt.2023.114628 · Cited by 35
Sensitization to PR-10 proteins is indicative of distinctive sensitization patterns in adults with a suspected food allergy
Blankestijn, M. A., Knulst, A. C., Knol, E. F., Le, T., Röckmann, H., Otten, H. G., & Klemans, R. J. B. (2017) · Clinical and Translational Allergy · doi:10.1186/s13601-017-0177-4 · Cited by 35
Lipid emulsion enhances fish allergen parvalbumin’s resistance to in vitro digestion and IgG/IgE binding capacity
Luo, C., Guo, Y., Li, Z., Ahmed, I., Pramod, S. N., Gao, X., Lv, L., & Lin, H. (2019) · Food Chemistry · doi:10.1016/j.foodchem.2019.125333 · Cited by 35
Contribution of Molecular Allergen Analysis in Diagnosis of Milk Allergy
Bartuzi, Z., Cocco, R. R., Muraro, A. M., & Nowak-Wegrzyn, A. H. (2017) · Current Allergy and Asthma Reports · doi:10.1007/s11882-017-0716-z · Cited by 34
Influence of the Carbohydrate Moieties on the Immunoreactivity and Digestibility of the Egg Allergen Ovomucoid
Benedé, S., López-Fandiño, R., Reche, M., Molina, E., & López-Expósito, I. (2013) · PLoS ONE · doi:10.1371/journal.pone.0080810 · Cited by 33
“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].”
Background
Changes in peptic digestibility of bovine β-lactoglobulin as a result of food processing studied by capillary electrophoresis and immunochemical methods
Maier, I., Okun, V. M., Pittner, F., & Lindner, W. F. (2006) · Journal of Chromatography B · doi:10.1016/j.jchromb.2006.06.040 · Cited by 33
Nutritional and Safety Assessments of Foods and Feeds Nutritionally Improved through Biotechnology: Case Studies: Executive Summary of a Task Force Report by the International Life Sciences Institute, Washington, D.C.
(2007) · Journal of Food Science · doi:10.1111/j.1750-3841.2007.00579.x · Cited by 32
High level expression, purification and physico- and immunochemical characterisation of recombinant Pen a 1: a major allergen of shrimp.
Albrecht, M., Alessandri, S., Conti, A., Reuter, A., Lauer, I., Vieths, S., & Reese, G. (2008) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.200700424 · Cited by 30
Mapping of a conformational epitope on the cashew allergen Ana o 2: A discontinuous large subunit epitope dependent upon homologous or heterologous small subunit association
Xia, L., Willison, L. N., Porter, L. L., Robotham, J. M., Teuber, S. S., Sathe, S. K., & Roux, K. H. (2010) · Molecular Immunology · doi:10.1016/j.molimm.2010.01.018 · Cited by 31
Are Dietary Lectins Relevant Allergens in Plant Food Allergy?
Barre, A., Damme, E. J. M. V., Simplicien, M., Benoist, H., & Rougé, P. (2020) · Foods · doi:10.3390/foods9121724 · Cited by 30
Food additives
Zeece, M. G. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-809434-1.00007-4 · Cited by 30
Stability of sunflower 2S albumins and LTP to physiologically relevant in vitro gastrointestinal digestion
Berecz, B., Mills, E. N. C., Parádi, I., Láng, F., Tamás, L., Shewry, P. R., & Mackie, A. R. (2012) · Food Chemistry · doi:10.1016/j.foodchem.2012.12.034 · Cited by 30
“This ability to bind lipid affects the stability of some LTPs and their resistance to hydrolysis (Breiteneder & Mills, 2005; Douliez et al., 2000; Vassilopoulou et al., 2006).”
BackgroundSelf-citation
Microbial Population, Physicochemical Quality, and Allergenicity of Molluscs and Shrimp Treated with Cobalt-60 Gamma Radiation
Sinanoglou, V. J., Batrinou, A., Konteles, S. J., & Sflomos, K. (2007) · Journal of Food Protection · doi:10.4315/0362-028x-70.4.958 · Cited by 30
“The latter is enhanced by an ability to bind ligands, such as metal ions, lipids, or steroids (3).”
Background
Assessment of Lupin Allergenicity in the Cholera Toxin Model: Induction of IgE Response Depends on the Intrinsic Properties of the Conglutins and Matrix Effects
Foss, N., Duranti, M. M., Magni, C., & Frøkiær, H. (2006) · International Archives of Allergy and Immunology · doi:10.1159/000094716 · Cited by 30
Effect of heat treatment on the conformational stability of intact and cleaved forms of the peanut allergen Ara h 6 in relation to its IgE-binding potency
de Jongh, H. H. J., de Jong, G. A. H., Apostolović, D., Taylor, S. L., Baumert, J. L., & Koppelman, S. J. (2020) · Food Chemistry · doi:10.1016/j.foodchem.2020.127027 · Cited by 29
Purification, Characterization, and Three-Dimensional Structure Prediction of Paramyosin, a Novel Allergen of Rapana venosa
Yu, C., Gao, X., Lin, H., Xu, L., Ahmed, I., Khan, M. U., Xu, M., Chen, Y., & Li, Z. (2020) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.0c04418 · Cited by 29
Use of Foodomics for Control of Food Processing and Assessing of Food Safety
Josić, D., Peršurić, Ž., Rešetar, D., Martinović, T., Saftić, L., & Kraljević Pavelić, S. (2017) · Advances in Food and Nutrition Research · doi:10.1016/bs.afnr.2016.12.001 · Cited by 28
Allergenicity of roasted peanuts treated with a non-human digestive protease
Yu, J., Hernandez, M. L., Li, H., Goktepe, I., Robinette, C., Auerbach, A., Peden, D. B., & Ahmedna, M. (2015) · Food Research International · doi:10.1016/j.foodres.2015.01.007 · Cited by 28
What Characteristics Confer Proteins the Ability to Induce Allergic Responses? IgE Epitope Mapping and Comparison of the Structure of Soybean 2S Albumins and Ara h 2
Han, Y., Lin, J., Bardina, L., Grishina, G. T., Lee, C., Seo, W. H., & Sampson, H. A. (2016) · Molecules · doi:10.3390/molecules21050622 · Cited by 28
“Many factors have been suggested to contribute to the overall allergenicity of any given protein, such as the number of IgE-binding epitopes, resistance to heat and proteolysis, the glycosylation status and enzymatic activity [1,2].”
Background
In-vitro-Diagnostik und molekulare Grundlagen von IgE-vermittelten Nahrungsmittelallergien
Kleine‐Tebbe, J., Ballmer-Weber, B. K., Beyer, K., Erdmann, S. M., Fuchs, T., Henzgen, M., Huttegger, I., Jappe, U., Jäger, L., Lepp, U. S., et al. (2009) · Allergologie · doi:10.5414/alp32177 · Cited by 28
Characterization of Relevant Biomarkers for the Diagnosis of Food Allergies: An Overview of the 2S Albumin Family
Bueno, C., Martín‐Pedraza, L., Parrón‐Ballesteros, J., Cuesta‐Herranz, J., Cabanillas, B., Pastor‐Vargas, C., Batanero, E., & Villalba, M. (2021) · Foods · doi:10.3390/foods10061235 · Cited by 27
“The disulfide bridges found in 2S albumins provide a compact structure that is stable to heat and enzymatic treatments [16,24].”
Background
Sensitization with 7S Globulins from Peanut, Hazelnut, Soy or Pea Induces IgE with Different Biological Activities Which Are Modified by Soy Tolerance
Kroghsbo, S., Bøgh, K. L., Rigby, N. M., Mills, E. N. C., Rogers, A., & Madsen, C. B. (2011) · International Archives of Allergy and Immunology · doi:10.1159/000321200 · Cited by 27
“Little is known about why some foods sensitizing via the gastrointestinal tract are prevalent allergenic foods and others are not. Factors such as eating habits, processing, and the food matrix have been suggested to influence the allergenicity of a given food [”
BackgroundSelf-citation
Effect of Roasting on the Conformational Structure and IgE Binding of Sesame Allergens
Ma, X., Li, H., Zhang, J., Ge, Y., He, L., Kang, W., Huang, W., Sun, J., & Chen, Y. (2022) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.2c01617 · Cited by 26
Fish β-parvalbumin acquires allergenic properties by amyloid assembly
Martínez, J., Sánchez, R., Castellanos, M., Fernández‐Escamilla, A. M., Vázquez‐Cortés, S., Fernández‐Rivas, M., & Gasset, M. (2015) · Swiss Medical Weekly · doi:10.4414/smw.2015.14128 · Cited by 26
Investigation on sequential extraction of peanut allergens for subsequent analysis by ELISA and 2D gel electrophoresis
Chassaigne, H., Brohée, M., Nørgaard, J., & van Hengel, A. J. (2007) · Food Chemistry · doi:10.1016/j.foodchem.2007.04.055 · Cited by 26
Quantification of the thaumatin‐like kiwi allergen by a monoclonal antibody‐based ELISA
Gavrović-Jankulović, M. Đ., Spasić, M., Veličković, T. Ć., Stojanović, M., Inić‐Kanada, A., Dimitrijević, L., Lindner, B., Petersen, A., Becker, W., & Jankov, R. (2008) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.200700286 · Cited by 26
“Pathogenesis-related (PR) proteins represent a very important, structurally heterogeneous group of plant allergens [36].”
Background
Allergenic Diversity among Plant and Animal Food Proteins
Kumar, S., Verma, A. K., Das, M., & Dwivedi, P. D. (2012) · Food Reviews International · doi:10.1080/87559129.2011.635391 · Cited by 26
“Similarly, there is evidence that nsLTPs can interact with lipid structures as well.(55) A propensity of certain proteins to aggregate might affect their ability to sensitize by generally enhancing their”
Background
Pine nut allergy: Clinical features and major allergens characterization
Cabanillas, B., Cheng, H., Grimm, C. C., Hurlburt, B. K., Rodríguez, J., Crespo, J. F., & Maleki, S. J. (2012) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201200245 · Cited by 25
“The 2S albumins are compact molecules because of the presence of four conserved disulfide bonds that exhibit high thermostability and resistance to extreme pH and proteolysis [19].”
Background
Modulation of gastrointestinal digestion of β-lactoglobulin and micellar casein following binding by (−)-epigallocatechin-3-gallate (EGCG) and green tea flavanols
Dönmez, Ö., Mogol, B. A., Gökmen, V., Tang, N., Andersen, M. L., & Chatterton, D. E. W. (2020) · Food & Function · doi:10.1039/d0fo00783h · Cited by 25
Research gaps and future needs for allergen prediction in food safety
Fernández, A., Danisman, E., Boroujerdi, M. T., Kazemi, S., Moreno, F. J., & Epstein, M. M. (2024) · Frontiers in Allergy · doi:10.3389/falgy.2024.1297547 · Cited by 24
Solution and high-pressure NMR studies of the structure, dynamics, and stability of the cross-reactive allergenic cod parvalbumin Gad m 1
Moraes, A. H., Ackerbauer, D., Kostadinova, M., Bublin, M., de Oliveira, G. A. P., Ferreira, F., Almeida, F. C. L., Breiteneder, H., & Valente, A. P. (2014) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.24664 · Cited by 24
Self-citation
Stability of allergen extracts used in skin testing and immunotherapy
Plunkett, G. A. (2008) · Current Opinion in Otolaryngology & Head & Neck Surgery · doi:10.1097/moo.0b013e3282ff62b0 · Cited by 24
Effect of egg white fermentation with lactobacilli on IgE binding ability of egg white proteins
Li, S., Offengenden, M., Fentabil, M. A., Gänzle, M. G., & Wu, J. (2013) · Food Research International · doi:10.1016/j.foodres.2013.03.018 · Cited by 26
Active actinidin retains function upon gastro‐intestinal digestion and is more thermostable than the E‐64‐inhibited counterpart
Grozdanović, M. M., Ostojić, S., Aleksić, I., Andjelković, U., Petersen, A., & Gavrović-Jankulović, M. Đ. (2014) · Journal of the Science of Food and Agriculture · doi:10.1002/jsfa.6656 · Cited by 24
Release of Major Peanut Allergens from Their Matrix under Various pH and Simulated Saliva Conditions—Ara h2 and Ara h6 Are Readily Bio-Accessible
Koppelman, S. J., Smits, M., Tomassen, M. M. M., de Jong, G. A. H., Baumert, J. L., Taylor, S. L., Witkamp, R. F., Veldman, R. J., Pieters, R. H. H., & Wichers, H. J. (2018) · Nutrients · doi:10.3390/nu10091281 · Cited by 24
“Ara h2 and Ara h6 are small (15–20 kDa) monomeric proteins [36,37], while Ara h1 and Ara h3 are larger and form complexes up to 180–700 kDa and 360–380 kDa, respectively [38–40].”
Background
Molecular Cloning, Mass Spectrometric Identification, and Nutritional Evaluation of 10 Coixins in Adlay (Coix lachryma-jobi L.)
Lin, L., Hsiao, E. S. L., Tseng, H.-S., Chung, M., Chua, A. C. N., Kuo, M.-E., & Tzen, J. T. C. (2009) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf903025n · Cited by 24
The Major Soybean Allergen Gly m Bd 28K Induces Hypersensitivity Reactions in Mice Sensitized to Cow’s Milk Proteins
Candreva, Á. M., Smaldini, P., Curciarello, R., Fossati, C. A., Docena, G. H., & Petruccelli, S. (2016) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.5b05623 · Cited by 23
Genetics of food allergy
Dreskin, S. C. (2006) · Current Allergy and Asthma Reports · doi:10.1007/s11882-006-0012-9 · Cited by 24
Allergenic sensitization versus elicitation risk criteria for novel food proteins
Herman, R. A., & Ladics, G. S. (2018) · Regulatory Toxicology and Pharmacology · doi:10.1016/j.yrtph.2018.02.016 · Cited by 22
Seed Storage Protein, Functional Diversity and Association with Allergy
Jain, A. (2023) · Allergies · doi:10.3390/allergies3010003 · Cited by 21
“The member of the cupin and prolamin families are among the group of proteins that are associated with food allergies [24].”
BackgroundInfluential
Foodomic investigations of food allergies
Andjelković, U., Martinović, T., & Josić, D. (2015) · Current Opinion in Food Science · doi:10.1016/j.cofs.2015.06.003 · Cited by 21
The impact of structural integrity and route of administration on the antibody specificity against three cow’s milk allergens - a study in Brown Norway rats
Madsen, J. L., Kroghsbo, S., Madsen, C., Pozdnyakova, I., Barkholt, V., & Bøgh, K. (2014) · Clinical and Translational Allergy · doi:10.1186/2045-7022-4-25 · Cited by 16
“These allergens possess different protein chemical features, some of which may influence their allergy-inducing capacity in quantity as well as quality, such as structural stability to processing, including digestion [15-18].”
Background
Identification and Characterization of β-Lathyrin, an Abundant Glycoprotein of Grass Pea ( Lathyrus sativus L.), as a Potential Allergen.
Xu, Q.-L., Song, B., Liu, F.-J., Song, Y.-Q., Chen, P., Liu, S.-S., & Krishnan, H. (2018) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.8b02314 · Cited by 19
Effects of deglycosylation and the Maillard reaction on conformation and allergenicity of the egg ovomucoid
Ma, J., Zhou, J., Chen, L., Zhang, H., Wang, Y., & Fu, L. (2021) · Journal of Food Science · doi:10.1111/1750-3841.15791 · Cited by 20
Isolation and characterization of a 28 kDa major allergen from blackgram (Phaseolus mungo)
Kumari, D., Arora, N., Kasera, R., Sridhara, S., Kumar, R., & Singh, B. (2012) · Immunobiology · doi:10.1016/j.imbio.2011.12.011 · Cited by 20
Overview of Plant Chitinases Identified as Food Allergens
Volpicella, M., Leoni, C., Fanizza, I., Placido, A., Pastorello, E. A., & Ceci, L. R. (2014) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf5007962 · Cited by 20
Novel foods and allergy: Regulations and risk-benefit assessment
van Putten, M. C., Kleter, G. A., Gilissen, L. J. W., Gremmen, B., Wichers, H. J., & Frewer, L. J. (2010) · Food Control · doi:10.1016/j.foodcont.2010.08.002 · Cited by 20
“No safety or risk assessment procedure can lead to the guaranteed safety of novel foods for food-allergic consumers, as the allergenicity of any given food or protein cannot be precluded completely, although the list of major food allergens is relatively limited (Breiteneder & Mills, 2005).”
Background
Antigenic cross‐reactivity between Schistosoma mansoni and peanut: a role for cross‐reactive carbohydrate determinants (CCDs) and implications for the hygiene hypothesis
Igetei, J. E., El-Faham, M. H., Liddell, S., & Doenhoff, M. J. (2017) · Immunology · doi:10.1111/imm.12711 · Cited by 19
In vitro gastrointestinal digestion of bovine αS1- and αS2-casein variants gives rise to different IgE-binding epitopes
Lisson, M., Lochnit, G., & Erhardt, G. (2013) · International Dairy Journal · doi:10.1016/j.idairyj.2013.06.012 · Cited by 19
Allergome: the characterization of allergens based on a 2D gel electrophoresis approach
Chardin, H., & Peltre, G. (2005) · Expert Review of Proteomics · doi:10.1586/14789450.2.5.757 · Cited by 19
Food-induced immunoglobulin E-mediated allergic rhinitis
Al-Rabia, M. (2015) · Journal of Microscopy and Ultrastructure · doi:10.1016/j.jmau.2015.11.004 · Cited by 19
Kinetic Stability of Proteins in Beans and Peas: Implications for Protein Digestibility, Seed Germination, and Plant Adaptation
Xia, K., Pittelli, S., Church, J., & Colón, W. (2016) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.6b01965 · Cited by 19
A Snapshot on Food Allergies: A Case Study on Edible Flowers
Lucarini, M., Copetta, A., Durazzo, A., Gabrielli, P., Lombardi‐Boccia, G., Lupotto, E., Santini, A., & Ruffoni, B. (2020) · Sustainability · doi:10.3390/su12208709 · Cited by 19
“It is noteworthy that, although the common structural characteristics of proteins and biological functions have been provisionally due to their immunogenicity, the prediction of the allergenicity of a protein cannot be based only on these two parameters [32].”
Background
Assessment of genetically modified maize NK603 × T25 × DAS‐40278‐9 and subcombinations, for food and feed uses, under Regulation (EC) No 1829/2003 (application EFSA‐GMO‐NL‐2019‐164)
(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., Naegeli, H., et al. (2021) · EFSA Journal · doi:10.2903/j.efsa.2021.6942 · Cited by 18
“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; Costa et al., 2021).”
Structural Database of Allergenic Proteins (SDAP)
Schein, C. H., Ivanciuc, O., & Braun, W. A. (2015) · ASM Press eBooks · doi:10.1128/9781555815721.ch11 · Cited by 18
Food allergy: begin at the skin, end at the mast cell?
Lukacs, N. W., & Hogan, S. P. (2025) · Nature reviews. Immunology · doi:10.1038/s41577-025-01185-y · Cited by 21
The severity of atopic dermatitis and analysis of the food hypersensitivity reactions
Čelakovská, J., & Bukač, J. (2015) · Food and Agricultural Immunology · doi:10.1080/09540105.2015.1043622 · Cited by 17
“Oral exposure to the food proteins is usually well tolerated because they are unstable in the presence of digestive enzymes (Breiteneder & Mills, 2005).”
Background
Allergic rhinitis caused by food allergies
Cingi, C., Demirbaş, D., & Songu, M. (2010) · European Archives of Oto-Rhino-Laryngology · doi:10.1007/s00405-010-1280-5 · Cited by 17
“Moreover, sensitisation to inhaled pollen proteins may result in cross-reactions with homologous fruit and vegetable proteins [20, 28].”
Influential
Insights from the pollination drop proteome and the ovule transcriptome ofCephalotaxusat the time of pollination drop production
Pirone-Davies, C., Prior, N., von Aderkas, P., SMITH, D. S. H., Hardie, D. B., Friedman, W. E., & Mathews, S. (2016) · Annals of Botany · doi:10.1093/aob/mcw026 · Cited by 16
Gaining perspective on the allergenicity assessment of genetically modified food crops
Goodman, R. E., & Hefle, S. L. (2005) · Expert Review of Clinical Immunology · doi:10.1586/1744666x.1.4.561 · Cited by 16
Rational Design, Structure–Activity Relationship, and Immunogenicity of Hypoallergenic Pru p 3 Variants
Eichhorn, S. P., Hörschläger, A., Steiner, M. J., Laimer, J., Jensen, B. M., Versteeg, S. A., Pablos, I., Briza, P., Zuidmeer, L., Rigby, N. M., et al. (2019) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201900336 · Cited by 16
Application of AllerCatPro 2.0 for protein safety assessments of consumer products
Krutz, N. L., Kimber, I., Winget, J. M., Nguyen, M. N., Limviphuvadh, V., Maurer‐Stroh, S., Mahony, C., & Gerberick, G. F. (2023) · Frontiers in Allergy · doi:10.3389/falgy.2023.1209495 · Cited by 15
Characterization and crystallization of a recombinant IgE Fab fragment in complex with the bovine β-lactoglobulin allergen
Niemi, M. H., Jänis, J., Jylhä, S., Kallio, J. M., Hakulinen, N., Laukkanen, M., Takkinen, K., & Rouvinen, J. (2007) · Acta Crystallographica Section F Structural Biology and Crystallization Communications · doi:10.1107/s174430910706160x · Cited by 15
“However, pollen and food allergens have been found to belong to only very few of the thousands of protein families (Breiteneder & Radauer, 2004; Breiteneder & Mills, 2005; Radauer & Breiteneder, 2006).”
Background
Assessment of genetically modified Maize MON 87429 for food and feed uses, under Regulation (EC) No 1829/2003 (application EFSA‐GMO‐NL‐2019‐161)
(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.2022.7589 · Cited by 15
“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).”
Purification, identification and preliminary crystallographic studies of Pru du amandin, an allergenic protein fromPrunus dulcis
Gaur, V., Sethi, D. K., & Salunke, D. M. (2007) · Acta Crystallographica Section F Structural Biology and Crystallization Communications · doi:10.1107/s1744309107064615 · Cited by 15
“Various biochemical and biophysical characteristics, such as thermal stability, pH stability, resistance to proteolysis, ligand interaction etc. have been associated with the allergenicity of proteins (Breiteneder & Mills, 2005).”
Background
Lipid transfer protein in diagnosis of birch–apple syndrome in children
Cudowska, B., Kaczmarski, M. G., & Restani, P. (2007) · Immunobiology · doi:10.1016/j.imbio.2007.07.006 · Cited by 15
Differential influence of the degree of processing on immunogenicity following proteolysis of casein and β-lactoglobulin
Sletten, G. B. G., Holden, L., Egaas, E., & Fæste, C. K. (2008) · Food and Agricultural Immunology · doi:10.1080/09540100802350963 · Cited by 15
“In general, interactions between allergens and other food components, are poorly understood, in particular their effects on the allergenicity of food proteins (Breiteneder & Mills, 2005).”
Background
Industrial dimensions of food allergy
Crevel, R. (2005) · Proceedings of The Nutrition Society · doi:10.1079/pns2005454 · Cited by 15
“Knowledge of the functional family to which a protein belongs can help form a judgement on the probability of it being allergenic, but is not sufficiently predictive on its own (Breiteneder & Mills, 2005).”
Background
Purification and Characterization of Naturally Occurring Post-Translationally Cleaved Ara h 6, an Allergen That Contributes Substantially to the Allergenic Potency of Peanut
de Jong, G. A. H., Jayasena, S., Johnson, P. E., Marsh, J. T., Apostolović, D., van Hage, M., Nordlee, J. A., Baumert, J. L., Taylor, S. L., Roucairol, C., et al. (2018) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.8b03140 · Cited by 14
Mapping of the Immunodominant Regions of Shrimp Tropomyosin Pan b 1 by Human IgE-Binding and IgE Receptor Crosslinking Studies
Myrset, H. R., Fæste, C. K., Kristiansen, P. E., & Dooper, M. M. B. W. (2013) · International Archives of Allergy and Immunology · doi:10.1159/000350791 · Cited by 14
Effect of Maillard reaction conditions on antigenicity of β-lactoglobulin and the properties of glycated whey protein during simulated gastric digestion
Li, Z., Luo, Y., Feng, L., & Liao, P. (2012) · Food and Agricultural Immunology · doi:10.1080/09540105.2012.712951 · Cited by 14
“…to possess allergenic potential. b-LG is very stabile against peptic digestion under acidic conditions, and this phenomenon is considered to correlate with its high allergenicity (Breiteneder & Mills, 2005; Maier, Okun, Pittner, & Lindner, 2006; Schmidt, Meijer, Slangen, & Van Beresteijn, 1995).”
Background
Immunostimulatory and allergenic properties of emulsified and non-emulsified digestion products of parvalbumin ( Scophthalmus maximus ) in RBL-2H3 cells and BALB/c mouse models
Luo, C., Chen, G., Ahmed, I., Sun, L., Li, W., Pavase, T. R., & Li, Z. (2021) · Food & Function · doi:10.1039/d1fo00575h · Cited by 13
An environmental ecocorona influences the formation and evolution of the biological corona on the surface of single-walled carbon nanotubes
Monikh, F. A., Chupani, L., Karkossa, I., Gardian, Z., Arenas-Lago, D., von Bergen�, M., Schubert, K. A., Piačková, V., Zusková, E., Jiskoot, W., et al. (2021) · NanoImpact · doi:10.1016/j.impact.2021.100315 · Cited by 13
Diversity in Seed Storage Proteins and Their Genes in Buckwheat
Chrungoo, N. K., Dohtdong, L., & Chettry, U. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-803692-1.00031-6 · Cited by 13
The value of position-specific scoring matrices for assessment of protein allegenicity
Lim, S. J., Tong, J. C., Chew, F. T., & Tammi, M. T. (2008) · BMC Bioinformatics · doi:10.1186/1471-2105-9-s12-s21 · Cited by 13
Food Allergens
Boye, J. I., Danquah, A., Thang, C., & Zhao, X. (2012) · doi:10.1002/9781118308035.ch42 · Cited by 13
Meat alternatives
Ismail, I., & Huda, N. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-91001-9.00004-9 · Cited by 12
Food hypersensitivity reactions in atopic dermatitis patients and analysis of contomitant diseases
Čelakovská, J., Bukač, J., & Ettler, K. (2014) · Food and Agricultural Immunology · doi:10.1080/09540105.2014.900531 · Cited by 12
“Oral exposure to the food proteins is usually well tolerated because they are unstable in the presence of digestive enzymes (Breiteneder & Mills, 2005).”
Background
High pressure processing of milk
Huppertz, T. (2010) · Elsevier eBooks · doi:10.1533/9781845699420.4.373 · Cited by 12
Assessment of genetically modified soybean GMB151 for food and feed uses, under Regulation (EC) No 1829/2003 (application EFSA‐GMO‐NL‐2018‐153)
(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.2021.6424 · Cited by 12
“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; Costa et al., 2021).”
Advances on the molecular characterization, clinical relevance, and detection methods of Gadiform parvalbumin allergens
Fernandes, T. J. R., Costa, J. S., Carrapatoso, I., Oliveira, M. B. P. P., & Mafra, I. (2015) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2015.1113157 · Cited by 12
Unraveling the mysteries of food allergens: aptamer-driven detection and suppression strategies.
Ding, M., Duan, M.-X., Wu, S.-J., & Duan, N. (2025) · Food Research International · doi:10.1016/j.foodres.2025.117021 · Cited by 10
Peanut allergens: new consolidated findings on structure, characteristics and allergom
Becker, W. M., Petersen, A., & Jappe, U. (2018) · Allergologie select · doi:10.5414/alx01418e · Cited by 11
“Another interesting observation is the fact that 11S-storage proteins tend to form aggregates, which when cooked can form gellike structures [13].”
Background
Enzyme- and nanozyme-based food allergen detections: from natural biocatalysts to rational engineering approaches
Wu, S., Zhao, J., Wang, Y., Raghavan, V., Dong, P., Zhang, X., Han, J., Wang, R., Tang, Y., Waterhouse, G. I. N., et al. (2025) · Trends in Food Science & Technology · doi:10.1016/j.tifs.2025.105016 · Cited by 11
Characterization of 2S albumin allergenic proteins for anaphylaxis in common buckwheat
Katsube‐Tanaka, T., & Monshi, F. I. (2022) · Food Chemistry Molecular Sciences · doi:10.1016/j.fochms.2022.100127 · Cited by 11
“T. Katsube-Tanaka and F.I. Monshi Food Chemistry: Molecular Sciences 5 (2022) 100127 and proteolytic denaturation (Breiteneder and Mills, 2005).”
Disulfide-related proteomic studies on food allergens
Yano, H. (2009) · Expert Review of Proteomics · doi:10.1586/epr.09.64 · Cited by 11
Purification of soybean cupins and comparison of IgE binding with peanut allergens in a population of allergic subjects
Ramadan, S., Marsh, J. T., El-Sherbeny, G. A., El‐Halawany, E. F., Luan, F., Baumert, J. L., Johnson, P. E., Osman, Y. A., & Goodman, R. E. (2020) · Food and Chemical Toxicology · doi:10.1016/j.fct.2020.111866 · Cited by 11
Change in conformational, digestive and immunological characteristics of bovine allergen β-lactoglobulin induced by metal ions in combination with heating
Fei, S., Zhou, J., Wu, Y., Tong, P., Gao, J., Chen, H., & Li, X. (2021) · Food Chemistry · doi:10.1016/j.foodchem.2021.130030 · Cited by 11

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

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Molecular properties of food allergens

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks