Structure and Function of the Peanut Panallergen Ara h 8

Hurlburt, Barry K.; Celeste, L.R.; Majorek, K.A.; McBride, Jane; Maleki, Soheila J.; Minor, W.; Chruszcz, M.

doi:10.1016/j.jaci.2012.12.748

Cited by 8 publications

(11 citation statements)

References 28 publications

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“…A recent study revealed a higher IgE binding response for Ara h 8 among a U.S. population where 2.4% of children, 49.4% of adolescents, and 42.9% of adults produced IgE against Ara h 8 (Valcour et al., ), suggesting this requires further serious study. Ara h 8 shares homology with other PR‐10 related allergens; for example, Api g 1, Dau c 1, Fra a 1, Gly m 4, and Pru av 1 (Hurlburt et al., ). Five linear antigenic epitopes and three conformational epitopes were predicted for Ara h 8 on a prediction modeling basis (Mishra et al., ).…”

Section: Molecular Characteristics Of Peanut Allergensmentioning

confidence: 99%

“…The Ara h 8 structure is composed of three α‐helices that flank a seven‐stranded anti‐parallel β‐sheet creating a large cavity with a metal binding site (sodium; Figure ). The most significant structural difference between Ara h 8 and other members of the Bet v 1 family was observed in the conformation of the β3, β4 strand, and the connecting loop between them (Hurlburt et al., ). Ara h 8 sequence was found to be most similar to Gly m 4, the soybean allergen, with 84% sequence similarity (Hurlburt et al., ).…”

Section: Molecular Characteristics Of Peanut Allergensmentioning

confidence: 99%

“…The most significant structural difference between Ara h 8 and other members of the Bet v 1 family was observed in the conformation of the β3, β4 strand, and the connecting loop between them (Hurlburt et al., ). Ara h 8 sequence was found to be most similar to Gly m 4, the soybean allergen, with 84% sequence similarity (Hurlburt et al., ). Although having low stability to heat (roasting) and very low stability to gastric digestion, Ara h 8 still possess IgE reactivity after heat treatment (Mittag et al., ).…”

Section: Molecular Characteristics Of Peanut Allergensmentioning

confidence: 99%

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Peanut Allergy: Characteristics and Approaches for Mitigation

Shah

Shi

Ashley

et al. 2019

Comp Rev Food Sci Food Safe

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Peanut allergy has garnered significant attention because of the high sensitization rate, increase in allergy, and severity of the reaction. Sufficiently reliable therapies and efficient mitigating techniques to combat peanut allergy are still lacking. Current management relies on avoiding peanuts and nuts and seeds with homologous proteins, although adverse events mostly occur with accidental ingestion. There is a need for hypoallergenic peanut products to protect sensitized individuals and perhaps serve as immunotherapeutic products. Alongside traditional practices of thermal and chemical treatment, novel processing approaches such as high‐pressure processing, pulsed ultraviolet light, high‐intensity ultrasound, irradiation, and pulsed electric field have been performed toward reducing the immunoreactivity of peanut. Covalent and noncovalent chemical modifications to proteins also have the tendency to alter peanut allergenicity. Enzymatic hydrolysis seems to be the most advantageous technique in diminishing the allergenic potential of peanut. Furthermore, the combined processing approach (hurdle technologies) such as enzymatic hydrolysis followed by, or in conjunction with, roasting, high pressure and heat, ultrasound with enzymatic treatment, or germination have shown a significant reduction of peanut immunoreactivity and may emerge as useful techniques in reducing the allergenicity of peanut and other foods. This study represents our current knowledge about the alterations in allergenic properties of peanut via different processing mechanisms as well as evaluating its future potential, geographical based data on increasing sensitization, clinical relevance, eliciting dose, and current management of peanut allergy. Furthermore, the molecular characteristics and clinical relevance of peanut allergens have been discussed.

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Section: Molecular Characteristics Of Peanut Allergensmentioning

confidence: 99%

Section: Molecular Characteristics Of Peanut Allergensmentioning

confidence: 99%

Section: Molecular Characteristics Of Peanut Allergensmentioning

confidence: 99%

See 1 more Smart Citation

Peanut Allergy: Characteristics and Approaches for Mitigation

Shah

Shi

Ashley

et al. 2019

Comp Rev Food Sci Food Safe

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“…These compounds are located in non-overlapping positions suggesting multiple ligands can bind simultaneously, similar to studies of ligand binding to the prototypical Bet v 1 [33]. Structural conservation of surface patches between Ara h 8 and the pollen allergen Bet v 1 may explain the IgE cross-reactivity between these panallergens [12]. …”

Section: Protein Structures Of Peanut Allergensmentioning

confidence: 94%

“…The structures of PR-10 proteins generally consist of a curved seven-stranded anti-parallel β-sheet flanked by three α-helices on one side creating a hydrophobic cavity with the ability to bind hydrophobic ligands [32]. Ara h 8 shares these structural features and has been shown to bind a number of biological compounds including flavonoids, suggesting a potential role as a flavonoid carrier protein [12]. Different crystal structures of recombinantly expressed Ara h 8 demonstrate binding of epicatechin as well as the laboratory buffer MES to the ligand-binding cavity (Fig.…”

Section: Protein Structures Of Peanut Allergensmentioning

confidence: 99%

The Molecular Basis of Peanut Allergy

Mueller

Maleki

Pedersen

2014

Curr Allergy Asthma Rep

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Peanut allergens can trigger a potent and sometimes dangerous immune response in an increasing number of people. The molecular structures of these allergens form the basis for understanding this response. This review describes the currently known peanut allergen structures and discusses how modifications both enzymatic and non-enzymatic affect digestion, innate immune recognition, and IgE interactions. The allergen structures help explain cross-reactivity among allergens from different sources, which is useful in improving patient diagnostics. Surprisingly, it was recently noted that related short peptide sequences among peanut allergens could also be a source of cross-reactivity. The molecular features of peanut allergens continue to inform predictions and provide new research directions in the study of allergic disease.

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