Identification of a major peanut allergen, I, in patients with atopic dermatitis and positive peanut challenges

Burks, A. Wesley; Williams, Larry W.; Helm, Ricki M.; Connaughton, Cathie; Cockrell, Gael; O'Brien, Thomas A.

doi:10.1016/0091-6749(91)90325-i

Cited by 318 publications

(192 citation statements)

References 26 publications

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“…Ara h 1 is a 63.5-kD glycoprotein that has significant homology with vicilin seed storage proteins in other legume plants (Burks et al, 1991(Burks et al, , 1995a. Ara h 1 has 40% similarity with soybean (Glycine max) and pea (Pisum sativum) vicilins at the protein level (Lycett et al, 1983), and 64% similarity with broad bean (Vicia faba) and pea vicilins at the DNA level (Burks et al, 1995b).…”

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confidence: 99%

Temporal and Spatial Expression of the Major Allergens in Developing and Germinating Peanut Seed

et al. 2007

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Peanut (Arachis hypogaea) seed proteins Ara h 1, Ara h 2, and Ara h 3 are considered to be the major peanut allergens. However, little is known about their temporal and spatial expression during seed development and upon germination and seedling growth. In this study, transcript levels of the three major peanut allergen genes, ara h 1, ara h 2, and ara h 3, and their corresponding proteins were found in all cultivars. Expression patterns were heterogeneous depending on the specific peanut allergen gene and the cultivars tested. However, ara h 3 expression patterns among the cultivars were more variable than ara h 1 and ara h 2. Transcripts were tissue specific, observed in seeds, but not in leaves, flowers, or roots, and were undetectable during seed germination. In situ hybridizations and immunotissue prints revealed that both embryonic axes and cotyledons expressed the allergens. However, more ara h 1 and ara h 3 messenger RNA was detected in cotyledons relative to embryonic axes. Allergen polypeptide degradation patterns were different in embryonic axes compared with cotyledons during germination and seedling growth, with levels of Ara h 1 and Ara h 2 dramatically reduced compared to the Ara h 3 polypeptides in embryonic axes. These characterization studies of major peanut allergen genes and their corresponding seed storage proteins can provide the basic information needed for biochemical and molecular approaches to obtain a hypoallergenic peanut.

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Temporal and Spatial Expression of the Major Allergens in Developing and Germinating Peanut Seed

et al. 2007

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“…A major allergen found in the cotyledon is the peanut protein, Ara h 1 [4]. The Ara h 1 allergen belongs to the vicilin family of seed storage proteins [5].…”

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confidence: 99%

“…The Ara h 1 allergen belongs to the vicilin family of seed storage proteins [5]. This protein is recognized by greater than 90% of peanut-sensitive patients, thus establishing it as an important allergen [4]. The majority of serum IgE recognition of the Ara h 1 allergen appears to be due to epitopes within this protein that are linear amino acid sequences that do not contain significant amounts of carbohydrate [4, combinant Ara h 1 protein and the native form of this allergen when individual patient serum was tested [S].…”

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confidence: 99%

Mapping and Mutational Analysis of the IgE‐Binding Epitopes on Ara h 1, a Legume Vicilin Protein and a Major Allergen in Peanut Hypersensitivity

Burks

Shin

Cockrell

et al. 1997

European Journal of Biochemistry

288

242

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Peanut allergy is a significant health problem because of the prevelance and potential severity of the allergic reaction. Serum IgE from patients with documented peanut hypersensitivity reactions and overlapping peptides were used to identify the IgE-binding epitopes on the major peanut allergen, Ara h 1. At least twenty-three different linear IgE-binding epitopes, located throughout the length of the Ara h 1 protein, were identified. All of the epitopes were 6-10 amino acids in length, but there was no obvious sequence motif shared by all peptides. Four of the peptides appeared to be immunodominant IgE-binding epitopes in that they were recognized by serum from more than 80% of the patients tested and bound more IgE than any of the other Ara h 1 epitopes. Mutational analysis of the immunodominant epitopes revealed that single amino acid changes within these peptides had dramatic effects on IgE-binding characteristics. The identification and determination of the IgE-binding capabilities of core amino acids in epitopes on the Ara h 1 protein will make it possible to address the pathophysiologic and immunologic mechanisms regarding peanut hypersensitivity reactions specifically and food hypersensitivity in general.

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“…Three peanut proteins Ara h 1, Ara h 2 and Ara h 3 are considered major allergens because they are recognized by more than 50% of peanuts allergic patients [26,27] . The three major allergens were present in the US commercial cultivar Georgia green and in the peanut cultivar collected in Côte d'Ivoire (ARA-CI) [28] .…”

Section: Discussionmentioning

confidence: 99%

Comparison of major peanut allergens Ara h 1, Ara h 2 and Ara h 3 between peanut cultivars from Côte d’Ivoire and the USA using SDS PAGE and Western Blots

Yapo-Crezoit¹,

Ananga²,

Yapo³

et al. 2017

IOSRJPBS

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Identification of a major peanut allergen, I, in patients with atopic dermatitis and positive peanut challenges

Cited by 318 publications

References 26 publications

Temporal and Spatial Expression of the Major Allergens in Developing and Germinating Peanut Seed

Temporal and Spatial Expression of the Major Allergens in Developing and Germinating Peanut Seed

Mapping and Mutational Analysis of the IgE‐Binding Epitopes on Ara h 1, a Legume Vicilin Protein and a Major Allergen in Peanut Hypersensitivity

Comparison of major peanut allergens Ara h 1, Ara h 2 and Ara h 3 between peanut cultivars from Côte d’Ivoire and the USA using SDS PAGE and Western Blots

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