peanut hypersensitivity/protease

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Proteolysis of the peanut allergen Ara h 1 by an endogenous aspartic protease.

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The 7S and 11S globulins of peanuts are subjected to proteolysis two days after seed imbibition, with Ara h 1 and the arachin acidic chains being among the first storage proteins to be mobilized. Proteolytic activity was greatest at pH 2.6-3 and is inhibited by pepstatin A, characteristic of an

Evaluation of nanoparticles as oral vehicles for immunotherapy against experimental peanut allergy.

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The aim of this work was to evaluate the potential application of an original oral immunotherapy, based on the use of nanoparticles, against an experimentally induced peanut allergy. In this context, a roasted peanut extract, containing the main allergenic proteins, were encapsulated into

Genetic diversity between mouse strains allows identification of the CC027/GeniUnc strain as an orally reactive model of peanut allergy.

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BACKGROUND Improved animal models are needed to understand the genetic and environmental factors that contribute to food allergy. OBJECTIVE We sought to assess food allergy phenotypes in a genetically diverse collection of mice. METHODS We selected 16 Collaborative Cross (CC) mouse strains, as well

Hepatic Mitochondrial Dysfunction and Immune Response in a Murine Model of Peanut Allergy.

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BACKGROUND Evidence suggests a relevant role for liver and mitochondrial dysfunction in allergic disease. However, the role of hepatic mitochondrial function in food allergy is largely unknown. We aimed to investigate hepatic mitochondrial dysfunction in a murine model of peanut

Structure and stability of 2S albumin-type peanut allergens: implications for the severity of peanut allergic reactions.

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Resistance to proteolytic enzymes and heat is thought to be a prerequisite property of food allergens. Allergens from peanut (Arachis hypogaea) are the most frequent cause of fatal food allergic reactions. The allergenic 2S albumin Ara h 2 and the homologous minor allergen Ara h 6 were studied at

Evaluating pH-induced gastrointestinal aggregation of Arachis hypogaea 1 fragments as potential components of peanut allergy.

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The seed storage glycoprotein Arachis hypogaea (Ara h) 1 is a major allergen found in peanuts. The biochemical resistance of food proteins to protease digestion contributes to their allergenicity. The rapid proteolysis of Ara h 1 under gastric conditions challenges this model. Biophysical and in

Structure of the major peanut allergen Ara h 1 may protect IgE-binding epitopes from degradation.

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In the past decade, there has been an increase in allergic reactions to peanut proteins, sometimes resulting in fatal anaphylaxis. The development of improved methods for diagnosis and treatment of peanut allergies requires a better understanding of the structure of the allergens. Ara h 1, a major

Role of complement in a murine model of peanut-induced anaphylaxis.

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Peanut allergy is severe and persisting from childhood to adulthood. However, there is no effective prophylaxis or treatment for peanut allergy. Little is known to about the molecular process in the pathogenesis of peanuts allergy, especially in innate immunity. Thus we investigated the role of

Cross-allergic reactions to legumes in lupin and fenugreek-sensitized mice.

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Several legumes may induce allergy, and there is extensive serological cross-reactivity among legumes. This cross-reactivity has traditionally been regarded to have limited clinical relevance. However, the introduction of novel legumes to Western countries may have changed this pattern, and in some

Anaphylactic reactions in mice with Fenugreek allergy.

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Fenugreek is a legume mostly used as a spice in Indian-style cooking. Although it has been used since ancient times, its allergenicity has only been reported in the last two decades. It poses special problems as an emerging and often hidden allergen. Fenugreek exposure may have serious implications

A single oral sensitization to peanut without adjuvant leads to anaphylaxis in mice.

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BACKGROUND A model of peanut food allergy has been developed in mice using a simple sensitization protocol leading to a quantitatively measurable allergic response. METHODS C3H/HeJ mice received a single intragastric administration of whole peanut (80 mg) without adjuvant. Two weeks later,

Bis(tributyltin)oxide (TBTO) decreases the food allergic response against peanut and ovalbumin in Brown Norway rats.

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Other factors than the allergen itself may be of importance in the development of food allergy. This report describes the influence of the immunosuppressive compound bis(tributyltin)oxide (TBTO), present in the food chain, on the development of food allergy to peanut or ovalbumin in Brown Norway

Epicutaneous immunotherapy protects cashew sensitized mice from anaphylaxis

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Background: The prevalence of tree nut allergy has increased worldwide, and cashew has become one of the most common food allergens. More critically, cashew allergy is frequently associated with severe anaphylaxis. Despite the high

Chapter 23: Food allergy.

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The onset of IgE-mediated food allergy is usually within minutes to 2 hours of food ingestion. Risk factors for fatal food-induced anaphylaxis include presence of asthma (which is a risk factor for anaphylaxis in general), failure to use epinephrine autoinjectors promptly, history of prior severe

Food allergy: Diagnosis and treatment.

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Immunoglobulin E-mediated food reactions usually develop within minutes of food ingestion. Although most reactions are not life-threatening, fatalities do occur. Risk factors for fatal food-induced anaphylaxis include the presence of asthma (a risk factor for anaphylaxis in general), failure to use

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