The importance of the 2S albumins for allergenicity and cross-reactivity of peanuts, tree nuts, and sesame seeds

2020 ◽  
Author(s):  
Stephen C. Dreskin ◽  
Stef J. Koppelman ◽  
Sandra Andorf ◽  
Kari C. Nadeau ◽  
Anjeli Kalra ◽  
...  
Keyword(s):  
Cross Reactivity ◽  
Sesame Seeds ◽  
Tree Nuts ◽  
2S Albumins

scholarly journals Common food allergens and cross-reactivity

2020 ◽  
Vol 2 (1) ◽  
pp. 17-21
Author(s):  
Olivia L. Francis ◽  
Kathleen Y. Wang ◽  
Edwin H. Kim ◽  
Timothy P. Moran
Keyword(s):  
Food Allergy ◽  
Protein Stability ◽  
Cross Reactivity ◽  
Molecular Characteristics ◽  
Food Allergens ◽  
Tree Nuts ◽  
Heat Stable ◽  
Systemic Reactions ◽  
Hen’S Egg ◽  
Fish And Shellfish

The most clinically relevant food allergens are cow’s milk, hen’s egg, peanut, tree nuts, wheat, soy, fish, shellfish, and seeds. Heat-stable food allergens have molecular characteristics that enhance protein stability and gastrointestinal absorption and thus are more likely to cause systemic reactions on ingestion. In contrast, heat-labile food allergens lack these characteristics and do not typically elicit reactions if sufficiently altered by heat or acid. Immunologic cross-sensitization between food allergens is more common than clinical cross-reactivity. However, certain groups of food allergens, such as tree nuts, fish, and shellfish, are associated with high rates of clinical cross-reactivity. Knowing the rates of clinical cross-reactivity is important when providing guidance to patients with food allergy and families on what foods can be safely added to the diet and what foods should be avoided.

scholarly journals The 11S globulin Sin a 2 from yellow mustard seeds shows IgE cross-reactivity with homologous counterparts from tree nuts and peanut

2012 ◽  
Vol 2 (1) ◽  
pp. 23 ◽  
Author(s):  
Sofía Sirvent ◽  
Martial Akotenou ◽  
Javier Cuesta-Herranz ◽  
Andrea Vereda ◽  
Rosalía Rodríguez ◽  
...  
Keyword(s):  
Cross Reactivity ◽  
Yellow Mustard ◽  
Tree Nuts ◽  
11S Globulin ◽  
Mustard Seeds

Cross-Reactivity Among Almond, Peanut and Other Tree Nuts in Almond Allergic Patients

2006 ◽  
Vol 117 (2) ◽  
pp. S32 ◽  
Author(s):  
A. Kewalramani ◽  
S.J. Maleki ◽  
H. Cheng ◽  
S. Teuber
Keyword(s):  
Cross Reactivity ◽  
Tree Nuts

Cross-reactivity profiles of legumes and tree nuts using the xMAP® multiplex food allergen detection assay

2017 ◽  
Vol 409 (25) ◽  
pp. 5999-6014 ◽  
Author(s):  
Chung Y. Cho ◽  
Carolyn Oles ◽  
William Nowatzke ◽  
Kerry Oliver ◽  
Eric A.E. Garber
Keyword(s):  
Food Allergen ◽  
Cross Reactivity ◽  
Tree Nuts ◽  
Detection Assay ◽  
Allergen Detection

Seed storage 2S albumins are predictive indicators of exclusive Anacardiaceae cross‐reactivity

2019 ◽  
Vol 49 (4) ◽  
pp. 545-549 ◽  
Author(s):  
Cristina Bueno‐Díaz ◽  
Laura Martín‐Pedraza ◽  
Sara Benedé ◽  
Elisa Haroun‐Díaz ◽  
Manuel las Heras ◽  
...  
Keyword(s):  
Seed Storage ◽  
Cross Reactivity ◽  
2S Albumins ◽  
Predictive Indicators

scholarly journals Isotretinoin-associated exercise-induced anaphylaxis in a patient with birch pollinosis and soybean sensitization: case presentation and literature review

2021 ◽  
Vol 17 (1) ◽  
Author(s):  
Anna Bamidis ◽  
Silke C. Hofmann
Keyword(s):  
Literature Review ◽  
Acne Vulgaris ◽  
Birch Pollen ◽  
Pollen Allergy ◽  
Allergic Patient ◽  
Cross Reactivity ◽  
Case Presentation ◽  
Tree Nuts ◽  
Exercise Induced ◽  
Isotretinoin Therapy

Abstract Background Peanut and soybean allergies are listed as contraindication in the package leaflet of isotretinoin, a widely used treatment of acne vulgaris. Cross-reactivity between PR10-proteins in peanut, tree nuts, and soybean is particularly common in patients with birch pollinosis and may lead to anaphylactic reactions in sensitized patients after intake of soybean oil containing isotretinoin capsules. Case presentation Here, we describe a young man with hazelnut and birch pollen allergy, who experienced exercise-induced anaphylaxis after isotretinoin intake on the third day of treatment. A complete allergy work-up was carried out, and sensitization to both peanut and soybean PR10-proteins was confirmed. However, oral provocation with isotretinoin remained negative in the absence of intense physical activity and longterm treatment was well tolerated. Conclusion To our knowledge, this is the first report of an exercise-induced anaphylaxis due to isotretinoin therapy. Our literature review to assess tolerability of isotretinoin in patients allergic to peanut, tree nuts or soybean revealed only one other case of anaphylaxis in a cashew-nut allergic patient sensitized to soybean PR10-protein Gly m 4. While there are no reports on soybean allergic patients treated with isotretinoin, the vast majority of peanut or tree nut allergic patients tolerated isotretinoin. Therefore, we conclude that sensitization to soybean, peanut or tree nuts should not preclude isotretinoin therapy. Particular caution is however warranted in patients with soybean sensitization. Pre-treatment oral challenges with isotretinoin may be recommended and physicians should be aware of the potential role of cofactors.

scholarly journals Immunoglobulin E-Binding Pattern of Canadian Peanut Allergic Children and Cross-Reactivity with Almond, Hazelnut and Pistachio

Biomolecules ◽  
2020 ◽  
Vol 10 (8) ◽  
pp. 1091
Author(s):  
Mélanie Pitre ◽  
Lamia L’Hocine ◽  
Allaoua Achouri ◽  
Martin Blaquière ◽  
Anne Des Roches
Keyword(s):  
Storage Proteins ◽  
Immunoglobulin E ◽  
Reciprocal Inhibition ◽  
Cross Reactivity ◽  
2S Albumin ◽  
Tree Nuts ◽  
Cross Reactions ◽  
Inhibition Elisa ◽  
Serum Pool ◽  
Tree Nut

Peanut allergic individuals can be both co-sensitized and co-allergic to peanut and tree nuts. At the moment, standard diagnostic approaches do not always allow differentiation between clinically relevant sensitization and nonsignificant cross-reactions, and the responsibility of each allergen remains unclear. The objective of this study was therefore to determine a peanut sensitization profile in a cohort of Canadian peanut allergic children and assess the immunoglobulin E (IgE) molecular cross-reactivity between peanut, almond, hazelnut and pistachio. The specific IgE (sIgE) levels of each patient serum were determined by ImmunoCAP, indirect ELISA and immunoblot to examine their sIgE-binding levels and profiles to peanut proteins. Reciprocal inhibition ELISA and immunoblotting were used to study sIgE cross-reactions between peanut and the selected tree nuts using an adjusted and representative serum pool of the nine allergic patients. The results showed that the prepared peanut and tree nut protein extracts allowed for the detection of the majority of peanut and selected tree nut known allergens. The reciprocal inhibition ELISA experiments showed limited sIgE cross-reactivities between peanut and the studied tree nuts, with peanut being most likely the sensitizing allergen and tree nuts the cross-reactive ones. In the case of hazelnut and pistachio, a coexisting primary sensitization to hazelnut and pistachio was also demonstrated in the serum pool. Reciprocal inhibition immunoblotting further revealed that storage proteins (2S albumin, 7S vicilin and 11S legumin) could possibly account for the observed IgE-cross-reactions between peanut and the studied tree nuts in this cohort of allergic individuals. It also demonstrated the importance of conformational epitopes in the exhibited cross-reactions.

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