nut hypersensitivity/albumin

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The protein structure determines the sensitizing capacity of Brazil nut 2S albumin (Ber e1) in a rat food allergy model.

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: It is not exactly known why certain food proteins are more likely to sensitize. One of the characteristics of most food allergens is that they are stable to the acidic and proteolytic conditions in the digestive tract. This property is thought to be a risk factor in allergic sensitization. The

Isolation, cloning, and characterization of the 2S albumin: a new allergen from hazelnut.

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METHODS 2S albumins are the major allergens involved in severe food allergy to nuts, seeds, and legumes. We aimed to isolate, clone, and express 2S albumin from hazelnut and determine its allergenicity. METHODS 2S albumin from hazelnut extract was purified using size exclusion chromatography and

Ana o 3, an important cashew nut (Anacardium occidentale L.) allergen of the 2S albumin family.

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BACKGROUND Cashew nut allergy is the second most commonly reported tree nut allergy in the United States. We have previously cloned and characterized major cashew allergens belonging to the vicilin and legumin families of seed storage proteins. OBJECTIVE Here we set out to describe a third major

Pine nut allergy: clinical features and major allergens characterization.

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METHODS The aims of this study were to evaluate IgE-mediated hypersensitivity to pine nut with details of clinical reactions and to characterize major pine nut allergens. RESULTS The study included ten consecutive teenagers and adults diagnosed with IgE-mediated clinical allergy to pine nut. Two

Anaphylaxis to buckwheat in an atopic child: a risk factor for severe allergy to nuts and seeds?

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Common buckwheat (Fagopyrum esculentum) is known to cause severe anaphylactic reactions in adult individuals. However, type I allergy to buckwheat is rarely seen in children. We report on a 7-year-old boy who developed a grade III anaphylactic reaction after consumption of a cake containing

Decreased immunoglobulin E (IgE) binding to cashew allergens following sodium sulfite treatment and heating.

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Cashew nut and other nut allergies can result in serious and sometimes life-threatening reactions. Linear and conformational epitopes within food allergens are important for immunoglobulin E (IgE) binding. Methods that disrupt allergen structure can lower IgE binding and lessen the likelihood of

Linear IgE epitope mapping of the English walnut (Juglans regia) major food allergen, Jug r 1.

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BACKGROUND Peanut and tree nut allergies can be life-threatening, and they appear to be growing in prevalence. Jug r 1, a 2S albumin seed storage protein, was previously characterized as a major English walnut food allergen. OBJECTIVE We sought to identify the linear IgE-binding epitopes of Jug r 1

Epitopes With Similar Physicochemical Properties Contribute to Cross Reactivity Between Peanut and Tree Nuts

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Many individuals with peanut (PN) allergy have severe reactions to tree nuts (TN) such as walnuts or cashews. Although allergenic proteins in TN and PN have overall low identity, they share discrete sequences similar in physicochemical properties (PCP) to known IgE epitopes. Here, PCP-consensus

IgE Cross-Reactivity of Cashew Nut Allergens.

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BACKGROUND Allergic sensitisation towards cashew nut often happens without a clear history of eating cashew nut. IgE cross-reactivity between cashew and pistachio nut is well described; however, the ability of cashew nut-specific IgE to cross-react to common tree nut species and other Anacardiaceae,

Jug r 4, a legumin group food allergen from walnut (Juglans regia Cv. Chandler).

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Allergy to walnut is the most frequently reported tree nut allergy in the United States. Walnut 2S albumin, a vicilin-like protein, and a lipid transfer protein allergen have previously been described. Our objective was to clone and express a cDNA encoding a legumin group protein, assess IgE-binding

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