Conformational IgE-binding Epitopes of Major Peanut Allergen Ara h 2 Revealed with Chimeric 2S-albumins

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

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 peanut allergen belonging to the vicilin family of seed storage proteins, is recognized by serum I...

Homology modelling of the major peanut allergen Ara h 2 and surface mapping of IgE-binding epitopes.

Three-dimensional models built for the peanut Ara h 2 allergen and other structurally-related 2S albumin allergens of dietary nuts exhibited an overall three-dimensional fold stabilized by disulphide bridges well conserved among all the members of the 2S albumin superfamily. Conformational analysis of the linear IgE-binding epitopes mapped on the molecular surface of Ara h 2 showed no structura...

Recombinant peanut allergen Ara h I expression and IgE binding in patients with peanut hypersensitivity.

Peanut allergy is a significant health problem because of the frequency, the potential severity, and the chronicity of the allergic sensitivity. Serum IgE from patients with documented peanut hypersensitivity reactions and a peanut cDNA expression library were used to identify clones that encode peanut allergens. One of the major peanut allergens, Ara h I, was selected from these clones using A...

Peanut panallergen Ara h 8 IgE and IgG4 epitopes

IgE cross-reactivity between the major peanut allergen Ara h 2 and the non-homologous allergens Ara h 1 and Ara h 3

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 whether cosensitization to these 3 allergens is caused by IgE cross-reactivity, despite the fact that...