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peanut hypersensitivity/albumina
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Pagina 1 a partire dal 18 risultati
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
Immunochemical characterisation of structure and allergenicity of peanut 2S albumins using different formats of immunoassays.
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Proteins of the 2S albumin family, such as Ara h2 and Ara h6, are most frequently involved in peanut allergy. We have developed a reverse enzyme allergo-sorbent test (EAST) in which total serum IgE antibodies are first captured by immobilised anti-human IgE monoclonal antibodies, and then the
Utility of specific IgE to Ara h 6 in peanut allergy diagnosis.
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BACKGROUND
Specific IgE to Ara h 2 has been shown to be useful in the diagnosis of peanut allergy, whereas the peanut lipid transfer protein, Ara h 9, has been suggested to be responsible for peanut allergy in the Mediterranean population.
OBJECTIVE
To better characterize peanut allergy in children
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
Specific IgE to peanut 2S albumin Ara h 7 has a discriminative ability comparable to Ara h 2 and 6.
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BACKGROUND
Little is known on the clinical relevance of peanut 2S albumin Ara h 7.
OBJECTIVE
To investigate the discriminative ability of Ara h 7 in peanut allergy and assess the role of cross-reactivity between Ara h 2, 6 and Ara h 7 isoforms.
METHODS
Sensitization to recombinant peanut storage
Effect of heating and glycation on the allergenicity of 2S albumins (Ara h 2/6) from peanut.
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BACKGROUND
Peanut allergy is one of the most common and severe food allergies, and processing is known to influence the allergenicity of peanut proteins. We aimed to establish the effect of heating and glycation on the IgE-binding properties and biological activity of 2S albumins (Ara h 2/6) from
The 2S albumin allergens of Arachis hypogaea, Ara h 2 and Ara h 6, are the major elicitors of anaphylaxis and can effectively desensitize peanut-allergic mice.
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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
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
Immunoglobulin-E reactivity to a glycosylated food allergen (peanuts) due to interference with cross-reactive carbohydrate determinants in heavy drinkers.
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BACKGROUND
N-glycans in plant and invertebrate glycoproteins can induce extensive IgE cross-reactivity therefore limiting the specificity of in vitro allergy tests. IgE sensitization to N-glycans (cross-reactive carbohydrate determinants, CCDs) may be increased in heavy drinkers, who therefore show
IgE cross-reactivity between the major peanut allergen Ara h 2 and the nonhomologous allergens Ara h 1 and Ara h 3.
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BACKGROUND
Ara h 1, a vicilin; Ara h 2, a 2S albumin; and Ara h 3, a legumin, are major peanut allergens. Ara h 2 is an important predictor of clinical reactivity to peanut, but cosensitization to all 3 allergens is correlated with the severity of patients' symptoms.
OBJECTIVE
We investigated
Characterization of potential allergens in fenugreek (Trigonella foenum-graecum) using patient sera and MS-based proteomic analysis.
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BACKGROUND
Fenugreek is a legume plant used as an ingredient of curry spice. Incidents of IgE-mediated food allergy to fenugreek have been reported. Coincidence with allergy to peanut, a major food allergen, seems to be common suggesting a rather high rate of
High frequency of IgE sensitization towards kiwi seed storage proteins among peanut allergic individuals also reporting allergy to kiwi.
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UNASSIGNED
IgE sensitization to storage proteins from nuts and seed is often related to severe allergic symptoms. There is a risk of immunological IgE cross-reactivity between storage proteins from different species. The potential clinical implication of such cross-reactivity is that allergens other
Immune reactivities to peanut proteins, agglutinins, and oleosins.
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BACKGROUND
Certain individuals are sensitive enough to react to peanuts and peanut oil, sometimes with deadly effect. It is thus crucial to have an accurate testing methodology for the assessment of allergies and immune reactivities to peanuts and their components, such as agglutinins and oleosins.
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
2S protein Ara h 7.0201 has unique epitopes compared to other Ara h 7 isoforms and is comparable to 2S proteins Ara h 2 and 6 in basophil degranulation capacity.
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BACKGROUND
Screening for specific IgE against 2S albumin proteins Ara h 2 and 6 has good positive predictive value in diagnosing peanut allergy. From the third 2S member Ara h 7, 3 isoforms have been identified. Their allergenicity has not been elucidated.
OBJECTIVE
This study investigated the
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