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conglutin/hipersensitivitas
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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
Assessment of lupin allergenicity in the cholera toxin model: induction of IgE response depends on the intrinsic properties of the conglutins and matrix effects.
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BACKGROUND
The well-established murine model of IgE-mediated food allergy, based on oral administration of antigen and cholera toxin (CT), has within the previous years been used to evaluate various food proteins. Nonetheless, little knowledge on the factors that determine the allergenicity of food
Monoclonal antibodies against the candidate lupin allergens alpha-conglutin and beta-conglutin.
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BACKGROUND
The ingestion of dietary products containing sweet lupin (such as Lupinus albus or Lupinus angustifolius) has been reported to cause IgE-mediated allergic reactions. Recent studies have indicated lupin globulins as important IgE binding proteins. The aim of the present study was to
Characterization of IgE binding to lupin, peanut and almond with sera from lupin-allergic patients.
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BACKGROUND
The increasing number of applications of sweet lupins in food is paralleled by an increase in immunoglobulin E (IgE)-mediated allergic reactions to lupin proteins. In particular, lupin allergy seems to appear in patients with an existing peanut allergy. In the present study, IgE-binding
Characterization of the sensitization profile to lupin in peanut-allergic children and assessment of cross-reactivity risk.
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BACKGROUND
Case reports of allergy to lupin, due to primary sensitization or cross-reactions with other legumes, are increasing as a consequence of the augmented use of lupin flour in bakery, pasta formulations and other food items. The main allergens that have been associated with the sensitization
Proteomic analysis of lupin seed proteins to identify conglutin Beta as an allergen, Lup an 1.
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Lupin products may be valuable as human foods because of their high protein content and potential anticholesterolemic properties. However, a small percentage of the population is allergic to lupin. In this study, we use in vitro IgE binding and mass spectrometry to identify conglutin beta, a major
Narrow-Leafed Lupin Main Allergen β-Conglutin (Lup an 1) Detection and Quantification Assessment in Natural and Processed Foods.
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The increasing prevalence of lupin allergy as a consequence to the functional characteristics of a growing number of sweet lupin-derived foods consumption makes the imperious necessity to develop analytical tools for the detection of allergen proteins in foodstuffs. The current study developed a new
Lupin allergy: a hidden killer in the home.
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This review addresses the problem of lupin sensitization in the home environment. We summarize the data currently available on allergy to lupin, which has become, in recent years, a hidden killer in our homes. Since 2006, when lupin was included in European regulations as a food whose presence must
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
One- and two-dimensional electrophoretic identification of IgE-binding polypeptides of Lupinus albus and other legume seeds.
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The prevalence of food allergies in the world population requires integrated approaches to identify new potential allergens, especially those of plant origin. The aim of this work was the allergen in vitro analysis of Lupinus albus seed proteome, a promising food protein source, and the assessment
Rapid shotgun proteomic liquid chromatography-electrospray ionization-tandem mass spectrometry-based method for the lupin ( Lupinus albus L.) multi-allergen determination in foods.
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Allergy to lupin is a growing food safety problem because this legume, increasingly exploited in the food industry, is one of the allergens that, according to law, must be declared on the labels of food products in the European Union. In this context, a rapid targeted proteomic approach based on
Almond allergens: molecular characterization, detection, and clinical relevance.
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Almond ( Prunus dulcis ) has been widely used in all sorts of food products (bakery, pastry, snacks), mostly due to its pleasant flavor and health benefits. However, it is also classified as a potential allergenic seed known to be responsible for triggering several mild to life-threatening immune
Identification of a new natural Ara h 6 isoform and of its proteolytic product as major allergens in peanut.
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Numerous food allergens of plant origin belong to the 2S albumin family, including peanut Ara h 2. In addition to Ara h 2, several other conglutins related to 2S albumins are present in peanut seeds. We evaluated the allergenicity of different peanut conglutins as compared with Ara h 2. Several
Allergens of Arachis hypogaea and the effect of processing on their detection by ELISA.
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Food allergies are an emerging public health problem in industrialized areas of the world. They represent a considerable health problem in these areas because of the relatively high number of reported cases. Usually, food allergens are proteins or glycoproteins with a molecular mass ranging from 10
Identification of a specific IgE-binding protein from narrow-leafed lupin (L. Angustifolius) seeds.
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Since lupin has been introduced as a food ingredient on the market there are more and more reports concerning its allergenic properties. However, only few narrow-leafed lupin proteins have yet been characterized as specific IgE-binding molecules and identified. The aim of the study has been to find
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