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arachis villosa/hipersenzitivnost

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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

Acquisition of tolerance to egg and peanut in African food-allergic children with atopic dermatitis.

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There are no previous data on tolerance development in children with atopic dermatitis (AD) and concomitant food allergy in low- and middle-income settings.To determine the rate of tolerance acquisition to egg and peanut 5 years after diagnosing food

Strategies to mitigate peanut allergy: production, processing, utilization, and immunotherapy considerations.

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Peanut (Arachis hypogaea L.) is an important crop grown worldwide for food and edible oil. The surge of peanut allergy in the past 25 years has profoundly impacted both affected individuals and the peanut and related food industries. In response, several strategies to mitigate peanut allergy have

Ultrasensitive carbohydrate-peptide SPR imaging microarray for diagnosing IgE mediated peanut allergy.

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Severity of peanut allergies is linked to allergen-specific immunoglobulin E (IgE) antibodies in blood, but diagnostics from assays using glycoprotein allergen mixtures may be inaccurate. Measuring IgEs specific to individual peptide and carbohydrate epitopes of allergenic proteins is promising. We
BACKGROUND Peanut allergy is increasing at an alarming pace in developed countries. Peanut (Arachis hypogaea) is a common food in Cuba. Nevertheless, reported values of sensitization and symptom severity are usually low. As our objective, we carried out an evaluation of allergic sensitivity to
BACKGROUND Ara h 2 and Ara h 6, co-purified together in a 13-25 kD fraction (Ara h 2/6; 20 kD fraction) on gel filtration chromatography, account for the majority of effector activity in a crude peanut extract (CPE) when assayed with RBL SX-38 cells sensitized with IgE from human peanut allergic

Lipophilic Allergens, Different Modes of Allergen-Lipid Interaction and Their Impact on Asthma and Allergy.

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Molecular allergology research has provided valuable information on the structure and function of single allergenic molecules. There are several allergens in food and inhalant allergen sources that are able to interact with lipid ligands via different structural features: hydrophobic pockets,

Benefits and limitations of molecular diagnostics in peanut allergy: Part 14 of the series Molecular Allergology.

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Allergic reactions to peanut (Arachis hypogaea, Ara h) are caused by immunoglobulin E (IgE)-mediated sensitizations to various proteins. The stability and relative proportion of these proteins in peanut determine the risk of hazardous reactions. Hazardous sensitization to seed storage proteins [S2

The peanut allergy epidemic: allergen molecular characterisation and prospects for specific therapy.

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Peanut (Arachis hypogaea) allergy is a major cause of food-induced anaphylaxis, with increasing prevalence worldwide. To date, there is no cure for peanut allergy, and, unlike many other food allergies, it usually persists through to adulthood. Prevention of exposure to peanuts is managed through

Intramuscular testosterone in arachis oil is safe for boys with peanut allergy requiring pubertal induction.

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Hidden allergens in food products are, especially for peanut-allergic consumers, a serious problem because even low amounts (approximately 200 microg) of peanut can elicit allergic reactions. Undeclared peanut traces can be found in processed food products, because contaminations with peanut during

Molecular evolution of genes encoding allergen proteins in the peanuts genus Arachis: Structural and functional implications.

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Food allergies are severe immune responses to plant and animal products mediated by immunoglobulin E (IgE). Peanuts (Arachis hypogaea L.) are among the top 15 crops that feed the world. However, peanuts is among the "big eight food allergens", and allergies induced by peanuts are a

Size-selective fractionation and visual mapping of allergen protein chemistry in Arachis hypogaea.

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Peanuts (Arachis hypogaea) in addition to milk, eggs, fish, crustaceans, wheat, tree nuts, and soybean are commonly referred to as the "big eight" foods that contribute to the majority of food allergies worldwide. Despite the severity of allergic reactions and growing prevalence in children and

Crystal structure of peanut (Arachis hypogaea) allergen Ara h 5.

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Profilins from numerous species are known to be allergens, including food allergens, such as peanut ( Arachis hypogaea ) allergen Ara h 5, and pollen allergens, such as birch allergen Bet v 2. Patients with pollen allergy can also cross-react to peanut. Structural characterization of allergens will
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