vicilin/overgevoeligheid

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Patients with anaphylaxis to pea can have peanut allergy caused by cross-reactive IgE to vicilin (Ara h 1).

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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

Purification and characterization of the 7S vicilin from Korean pine (Pinus koraiensis).

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Pine nuts are economically important as a source of human food. They are also of medical importance because numerous pine nut allergy cases have been recently reported. However, little is known about the proteins in pine nuts. The purpose of this study was to purify and characterize pine nut storage

Vicilin and the basic subunit of legumin are putative chickpea allergens.

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IgE-mediated reactions to food allergens constitute a major health problem in industrialized countries. Chickpea is consumed in Mediterranean countries, and reportedly associated with IgE-mediated hypersensitivity reactions. However, the nature of allergic reactions to chickpea has not been

Identification and Assessment of the Potential Allergenicity of 7S Vicilins in Olive (Olea europaea L.) Seeds.

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Olive seeds, which are a raw material of interest, have been reported to contain 11S seed storage proteins (SSPs). However, the presence of SSPs such as 7S vicilins has not been studied. In this study, following a search in the olive seed transcriptome, 58 sequences corresponding to 7S vicilins were

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

Emerging Allergens in Goji Berry Superfruit: The Identification of New IgE Binding Proteins towards Allergic Patients' Sera.

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The goji berry (Lycium barbarum L.) (GB) is gaining increasing attention with high consumption worldwide due to its exceptional nutritional value and medicinal benefits displayed in humans. Beyond their beneficial properties, GBs contain renowned allergenic proteins, and therefore deserve

Isolated IgE reactivity to native walnut vicilin-like protein (nJug r 2) on ISAC™ microarray is due to cross-reactive carbohydrate epitopes.

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BACKGROUND The last version of the microarray-based testing ImmunoCAP ISAC 112™ includes the native walnut (Junglans regia) molecules 2S albumin (nJug r 1), vicilin (nJug r 2) and lipid transfer protein (nJug r 3). In view of the many unexpected cases of isolated positivity to nJug r 2 occurring in

Identification of Almond ( Prunus dulcis) Vicilin As a Food Allergen.

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Almond is one of the tree nuts listed by U.S. FDA as a food allergen source. A food allergen identified with patient sera has been debated to be the 2S albumin or the 7S vicilin. However, neither of these proteins has been defined as a food allergen. The purpose of this study was to clone, express,

Len c 1, a major allergen and vicilin from lentil seeds: protein isolation and cDNA cloning.

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BACKGROUND Lentils are among the main plant foods causing allergic reactions in pediatric patients in the Mediterranean area and in many Asian communities. However, very few reports have been devoted to identifying lentil allergens. Seed storage proteins of the vicilin family have been characterized

Expression, purification and crystallization of pecan (Carya illinoinensis) vicilin.

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Tree nuts are responsible for many cases of severe food allergies. The 7S seed storage protein vicilin has been identified as a food allergen in many kinds of tree nuts. The vicilin protein consists of an N-terminal low-complexity region with antimicrobial activity and a C-terminal domain that forms

Allergen Recognition Patterns in Walnut Allergy Are Age Dependent and Correlate with the Severity of Allergic Reactions.

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Walnut is an important elicitor of food allergy in children and adults with a high rate of severe reactions. Multicenter studies using a common clinical protocol and a comprehensive allergen are lacking.To investigate potential correlations between

Lupin and Other Potentially Cross-Reactive Allergens in Peanut Allergy.

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OBJECTIVE The presence of IgE cross-reactivity between peanut allergens and allergens from other legumes and tree nuts has been demonstrated, but the identification of the involved individual allergens is still limited. The aim of this review is to describe new allergenic findings, of potential

Clinical and Molecular Characterization of Walnut and Pecan Allergy (NUT CRACKER Study).

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Diagnostic methods for distinguishing walnut-allergic patients from walnut-sensitized but walnut-tolerant individuals are limited. Furthermore, characteristics of single walnut versus dual walnut-pecan allergy are lacking.To provide clinical and molecular

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

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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

Immunoglobulin E cross-reactivity between lupine conglutins and peanut allergens in serum of lupine-allergic individuals.

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BACKGROUND Lupine is used increasingly in food products. The development of lupine allergy in peanut-allergic patients is believed to occur as a result of cross-reactivity between lupine and peanut proteins. OBJECTIVE To investigate the degree of immunoglobulin (Ig) E cross-reactivity between

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