Food and Drug Reactions and AnaphylaxisPatients with anaphylaxis to pea can have peanut allergy caused by cross-reactive IgE to vicilin (Ara h 1)☆,☆☆
Section snippets
Patients
Three patients with a history of severe allergic reactions after ingestion of pea who had peanut-related symptoms were investigated in this study. Specific IgE levels to pea and peanut and total IgE levels were determined by using the CAP system FEIA (Pharmacia & Upjohn, Uppsala, Sweden). Skin prick tests with commercial pea and peanut extracts (ALK-Abelló, Nieuwegein, The Netherlands) were performed and recorded as described by Dreborg and Frew.22 Detailed histories of pea- and peanut-related
Patients
Patient characteristics are summarized in Table I. Pea-related symptoms consisted of symptoms of itching and tingling of the oral cavity or lips and dyspnea in all patients. Two patients (nos. 1 and 3) experienced additional symptoms, such as generalized urticaria and cardiovascular symptoms, resulting in faintness. This required attendance at an emergency department more than once. Ingestion of peanut also induced oral symptoms in all patients: in patient 1 this was accompanied by generalized
Discussion
Three patients with histories of severe anaphylaxis after ingestion of pea were investigated regarding their peanut-related symptoms. In one patient peanut-related symptoms were confirmed by means of DBPCFC. The other 2 patients were not challenged with peanut because they had convincing histories of peanut anaphylaxis (Table I). Looking at the specific IgE levels, skin prick test results, and the course of development of food-related symptoms in these patients, it is assumed that their
Acknowledgements
We thank W. J. Koers for his help in recruiting patients with pea allergy and R. Vlooswijk and R. van Biert for their assistance in Western blot and ELISA experiments.
References (31)
- et al.
Prevalence of food allergy and intolerance in the adult Dutch population
J Allergy Clin Immunol
(1994) Peanut anaphylaxis
J Allergy Clin Immunol
(1990)- et al.
An evaluation of the sensitivity of subjects with peanut allergy to very low doses of peanut protein: a randomized, double-blind, placebo-controlled food challenge study
J Allergy Clin Immunol
(1997) - et al.
Allergenicity of major component proteins of soybean determined by enzyme-linked immunosorbent assay (ELISA) and immunoblotting in children with atopic dermatitis and positive soy challenges
J Allergy Clin Immunol
(1988) - et al.
Cross-allergenicity of peanut and lupine: The risk of lupine allergy in patients allergic to peanuts
J Allergy Clin Immunol
(1999) - et al.
Allergy to lentils in Mediterranean pediatric patients
J Allergy Clin Immunol
(1999) - et al.
Allergenic cross-reactions among legume foods—an in vitro study
J Allergy Clin Immunol
(1987) - et al.
Identification of unique peanut and soy allergens in sera adsorbed with cross-reacting antibodies
J Allergy Clin Immunol
(1996) - et al.
The natural history of peanut allergy
J Allergy Clin Immunol
(1989) - et al.
Cross-allergenicity in the legume botanical family in children with food hypersensitivity
J Allergy Clin Immunol
(1989)
Cross-allergenicity in the legume botanical family in children with food hypersensitivity. II. Laboratory correlates
J Allergy Clin Immunol
The isolation of allergens from the green pea
J Allergy Clin Immunol
A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
Anal Biochem
Identification of a major peanut allergen, Ara h I, in patients with atopic dermatitis and positive peanut challenges
J Allergy Clin Immunol
Heat induced conformational changes of Ara h 1, a major peanut allergen, do not affect its allergenic properties
J Biol Chem
Cited by (97)
RuBisCO as a protein source for potential food applications: A review
2023, Food ChemistryIs pea our hidden allergen? An American pediatric case series
2023, Journal of Allergy and Clinical Immunology: GlobalA perspective on pea allergy and pea allergens
2021, Trends in Food Science and TechnologyCitation Excerpt :However, the prevalence of allergies to specific legumes varies widely with only peanuts and soybeans on the global list of commonly allergenic foods (Taylor & Baumert, 2015). Clinical cross-reactivity between legume species is rare and, even where cross-reactivity occurs, it is limited to a few species of legumes (Kakleas et al., 2020; Martinez San Ireneo et al., 2000; Peeters et al., 2007, 2009; Wensing et al., 2003). Peanut-allergic individuals are typically allergic only to peanuts and similar mono-reactivity was noted for soybean and pea (Bernhisel-Broadbent & Sampson, 1989).
New directions in stabilization, clarification, and fining
2021, Managing Wine Quality: Volume 2: Oenology and Wine QualityClinical Relevance of Cross-Reactivity in Food Allergy
2021, Journal of Allergy and Clinical Immunology: In PracticePlant Lectins: Bioactivities and Bioapplications
2018, Studies in Natural Products ChemistryCitation Excerpt :Crossallergy is based on epitope similarity among proteins from different organisms, i.e., crossallergy between organisms of different species is due to the presence of structurally homologous proteins, which are recognized by the same IgE antibodies. The high sequence homology observed among legume vicilins (peanut, soybean, pea, and lentil) has been claimed as responsible for the IgE crossreactivity detected among these grain legumes [51–53]. For example, the risk of crossed allergy between lupine and peanut was documented as early as 1994 [54].
- ☆
Supported by TNO Nutrition and Food Research.
- ☆☆
Reprint requests: Marjolein Wensing, MD, Department of Dermatology/Allergology G02.124, University Medical Centre Utrecht, Heidelberglaan 100, 3584 CX Utrecht, The Netherlands.