Patients with anaphylaxis to pea can have peanut allergy caused by cross-reactive IgE to vicilin (Ara h 1)
Open accessAbstract
Background Serologic cross-reactivity among legumes has been described; however, it is rarely clinically significant. In this study 3 patients with a history of anaphylaxis to pea are described who subsequently had symptoms after ingestion of peanut.Objective We investigated whether the peanut-related symptoms were due to cross-reactivity between pea and peanut proteins.Methods Peanut-related symptoms were documented according to case history or double-blind, placebo-controlled food challenge results. Skin prick tests were performed, and specific IgE levels were determined for pea and peanut with the CAP system FEIA. IgE-binding proteins in pea and peanut were identified by using immunoblot analysis. Cross-reactivity was studied by means of immunoblot and ELISA inhibition studies with whole extracts and purified allergens.Results Peanut-related symptoms consisted of oral symptoms in all patients, with additional urticaria and dyspnea or angioedema in 2 patients. All patients had a positive skin prick test response and an increased IgE level to pea and peanut. Immunoblotting revealed strong IgE binding to mainly vicilin in pea extract and exclusively to Ara h 1 in crude peanut extract. Immunoblot and ELISA inhibition studies with crude extracts, as well as purified proteins, showed that IgE binding to peanut could be inhibited by pea but not or only partially the other way around.Conclusion Clinically relevant cross-reactivity between pea and peanut does occur. Vicilin homologues in pea and peanut (Ara h 1) are the molecular basis for this cross-reactivity.
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Case studies have documented that some individuals with a proven peanut allergy have a reaction to pea protein.
“While not common, there have been case studies documented of those with a proven peanut allergy having a reaction to pea protein [189,190].”
From Plant Proteins: Assessing Their Nutritional Quality and Effects on Health and Physical Function (2020) · cites this paper as [190]
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Plant Lectins: Bioactivities and Bioapplications
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“As a matter of facts, cross-reactivities among some legume seeds, including soybean and peanut [7], soybean, lentil, pea and bean [8], lupin, pea and soybean [9], lupin and peanut [10], as well as with specific protein classes, such as pea and lentil vicilins and convicilins [11], pea and peanut vicilins [12], have be…”
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The fascinating world of molecular diagnosis in the management of food allergy: nondum matura est
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New directions in stabilization, clarification, and fining
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Molecular characterisation and heat-induced gelation of pea vicilin and legumin
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Development of an Animal Model to Evaluate the Allergenicity of Food Allergens
Ahrens, B., Quarcoo, D., Bühner, S., Reese, G., Vieths, S., & Hamelmann, E. H. (2014) · International Archives of Allergy and Immunology · doi:10.1159/000363109 · Cited by 19 · see citing works
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Is pea our hidden allergen? An American pediatric case series
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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 · see citing works
Protein from Vegetable Sources: A Focus on Pea Protein
Lefranc‐Millot, C., & Teichman‐Dubois, V. (2018) · doi:10.1002/9781119385332.ch10 · Cited by 18 · see citing works
Bielikowicz, K., Kostyra, H., Kostyra, E., Teodorowicz, M., Rigby, N. M., & Wojtacha, P. (2012) · Food Research International · doi:10.1016/j.foodres.2012.06.028 · Cited by 17 · see citing works
Armentia, A., Álvarez, R., Moreno‐González, V., Martín, B. G., Fernández, S., Martín, S., Moro, A., Vega, J. M., Barrios, A., Castillo, M., et al. (2020) · Contact Dermatitis · doi:10.1111/cod.13644 · Cited by 16 · see citing works
“Green peas are the most common processed vegetable consumed in the UK and United States.5,6 The following pea allergens have been characterized: Pis s 1, a 44 kDa protein; a 7S vicilin-like globulin5; Pis s 2, a 63 kDa protein; a convicilin5; Pis s IFR, an isoflavone reductase6; and Pis s 8 profilin.7 Total IgE-bindin…”
BackgroundAllergic reactivity of bambara groundnut (Vigna subterranea) proteins
Astuti, R. M., Palupi, N. S., & Zakaria, F. R. (2016) · Food and Agricultural Immunology · doi:10.1080/09540105.2015.1129601 · Cited by 15 · see citing works
“IgE cross-reactivity among legumes had been demonstrated (de Leon et al., 2005; Wensing et al., 2003).”
BackgroundEvaluation of scientific criteria for identifying allergenic foods of public health importance
van Bilsen, J. H. M., Ronsmans, S., Crevel, R., Rona, R. J., Przyrembel, H., Penninks, A., Contor, L., & Houben, G. F. (2010) · Regulatory Toxicology and Pharmacology · doi:10.1016/j.yrtph.2010.08.024 · Cited by 14 · see citing works
van Odijk, J., Sjölander, S., Brostedt, P., Borres, M. P., & Englund, H. (2017) · Clinical and Molecular Allergy · doi:10.1186/s12948-017-0073-4 · Cited by 12 · see citing works
Consommation croissante d’aliments contenant du pois jaune : un risque d’allergie ?
Dreyer, L. E., Astier, C., Dano, D., Hosotte, M., Jarlot‐Chevaux, S., Sergeant, P., & Kanny, G. (2013) · Revue française d'allergologie · doi:10.1016/j.reval.2013.11.007 · Cited by 12 · see citing works
Akhi, A., Rana, M. R., Islam, M. N., & Ahmed, T. (2025) · Journal of Food Processing and Preservation · doi:10.1155/jfpp/4986605 · Cited by 10 · see citing works
Safety Assessment of Plant-Derived Proteins and Peptides as Used in Cosmetics
Burnett, C. L., Boyer, I. J., Bergfeld, W. F., Belsito, D. V., Hill, R. A., Klaassen, C. D., Liebler, D. C., Marks, J. G., Shank, R. C., Slaga, T. J., et al. (2022) · International Journal of Toxicology · doi:10.1177/10915818221100700 · Cited by 10 · see citing works
“A clinical study examined 3 patients with a history of anaphylactic reactions to peas who subsequently developed signs of sensitization after ingesting peanuts.(46) All 3 patients had positive skin prick tests, as well as elevated serum levels of IgE antibodies against protein extracts of both peas and peanuts.”
BackgroundJeong, K. Y., Park, K. H., Lee, J., & Park, J. (2017) · Allergy Asthma and Immunology Research · doi:10.4168/aair.2017.9.5.417 · Cited by 10 · see citing works
“Clinically relevant cross-reactivity between the pea and the peanut was reported due to vicilin-homologous allergens, Pis s 1, and Ara h 1.(24) However, there is a low rate of clinical cross-reactivity among these vicilin belonged allergens.”
BackgroundNahrungsmittelassoziierte Anaphylaxie
Dölle-Bierke, S., Hompes, S., Grünhagen, J., & Worm, M. (2012) · Der Hautarzt · doi:10.1007/s00105-011-2265-z · Cited by 9 · see citing works
An alternative allergen risk management approach
Manning, L., & Soon, J. M. (2016) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2016.1185085 · Cited by 9 · see citing works
“plant foods had been reported, for example, IgE-binding crossreactivity between peanut, lentil (Len c 1), and pea (Pis s 1) was identified (L opez-Torrej on et al. 2003; Wensing et al. 2003).”
BackgroundBreiteneder, H. (2006) · Elsevier eBooks · doi:10.1533/9781845690557.1.21 · Cited by 8 · see citing works
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Molecular diagnosis of peanut allergy
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Determination of pea proteins allergenicity with the use Balb/c mouse
Szymkiewicz, A., & Jedrychowski, L. (2006) · Central European Journal of Immunology · Cited by 6 · see citing works
Processing Foods without Soybean Ingredients
Boye, J. I., L’Hocine, L., & Rajamohamed, S. H. (2010) · doi:10.1002/9780470644584.ch13 · Cited by 6 · see citing works
Biase, M. D., Caponio, G. R., Cifarelli, V., Lonigro, S. L., Pulpito, M., Grandolfo, C., Difonzo, G., Calligaris, S., Plazzotta, S., Tamma, G., et al. (2025) · Applied Food Research · doi:10.1016/j.afres.2025.101515 · Cited by 5 · see citing works
Lidzba, N., Arteaga, V. G., Schiermeyer, A., Havenith, H., Muranyi, I. S., Schillberg, S., Lehmann, J., & Ueberham, E. (2021) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.0c07177 · Cited by 5 · see citing works
Risk Assessment of Clinical Reactions to Legumes in Peanut-Allergic Children
Jensen, L. B., Andersen, M., Skov, P. S., Poulsen, L. K., & Bindslev‐Jensen, C. (2008) · World Allergy Organization Journal · doi:10.1097/wox.0b013e3181865f83 · Cited by 5 · see citing works
“Wensing et al(6) reported that patients sensitized to pea exhibited clinically relevant cross-reactivity to peanut where the protein responsible for the cross-reaction was vicilin (Ara h 1 in peanut).(6) A serological cross-reactivity is, however, not synonymous with allergic reactions in the patients.”
BackgroundPredicting the Allergenicity of Novel Proteins in Genetically Modified Organisms
Goodman, R. E., & Wise, J. (2015) · ASM Press eBooks · doi:10.1128/9781555815721.ch9 · Cited by 5 · see citing works
Lipid Emulsion Therapies and Type 1 Hypersensitivity Reactions: Risk Assessment and Management
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Allergenicity of plant proteins
L’Hocine, L., Pitre, M., & Achouri, A. (2024) · Elsevier eBooks · doi:10.1016/b978-0-323-91721-6.00014-1 · Cited by 4 · see citing works
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Immunoreactive properties of pea protein extract and its trypsin hydrolysates
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“These proteins determine not only the nutritional value of peas for humans and animals, but also the immunogenic and allergenic potential of pea proteins (Hayakawa et al., 1999; Wensing et al., 2003).”
BackgroundPhysicochemical and sensory properties of soymilk from five soybean lines
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Development and verification of PCR based assay to dectect and quantify garden pea lec gene
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Protein quaternary structure and aggregation in relation to allergenicity
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Ara h 6 complements Ara h 2 as an important marker for IgE reactivity to peanut
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“It was shown by cross-immunoinhibition that Ara h 1 lacks some of the IgE epitopes shared by the possible sensitizer pea vicilin (Wensing et al. 2003).”
BackgroundEffect of modifications of pea albumins on their immunoreactive properties
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Emerging Allergens and the Future
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Nanotechnology and Food Allergy
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Improving allergenicity risk assessment of novel foods
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- Authors
- Wensing, M., Knulst, A. C., Piersma, S., O'Kane, F., Knol, E. F., & Koppelman, S. J.
- Affiliations
- University Medical Center Utrecht (NL)
- Netherlands Organisation for Applied Scientific Research (NL)
- Venue
- Journal of Allergy and Clinical Immunology
- Publisher
- Elsevier BV
- Published
- 2003-02
- Volume
- 111
- Issue
- 2
- Pages
- 420-424
- ISSN
- 0091-6749 (ISSN-L)
- OpenAlex
- W2138747157
- Cited by
- 118
- References
- 33
- Citations by year
- 2026: 4 · 2025: 4 · 2024: 3 · 2023: 4 · 2022: 6 · 2021: 6 · 2020: 4 · 2019: 2 · 2018: 4 · 2017: 2 · 2016: 3 · 2015: 3 · 2014: 2 · 2013: 7 · 2012: 6
- FWCI
- 4.20
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Journal of Allergy and Clinical Immunology (publishedVersion)
- PubMed (publishedVersion)
- Socio-Environmental Systems Modeling (acceptedVersion)
- Data Archiving and Networked Services (DANS) (submittedVersion)
- Topics
- Health Sciences › Medicine › Immunology and Allergy › Food Allergy and Anaphylaxis Research
- Health Sciences › Medicine › Immunology and Allergy › Allergic Rhinitis and Sensitization
- Health Sciences › Medicine › Pharmacology › Drug-Induced Adverse Reactions
- Keywords
- peanut allergy, vicilin, Ara h 1, IgE binding, legume allergens, anaphylaxis, double-blind placebo-controlled food challenge, skin prick test, allergen inhibition
- MeSH terms
- Allergens, Anaphylaxis, Cross Reactions, Food Hypersensitivity, Humans, Immunoglobulin E, Arachis, Plant Proteins, Pisum sativum, Peanut Hypersensitivity, Seed Storage Proteins, In Vitro Techniques
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