Structural Biology of Peanut Allergens

Offermann, L.R.; Perdue, Makenzie L.; He, John Z.; Hurlburt, Barry K.; Maleki, Soheila J.; Chruszcz, M.

doi:10.7726/jci.2015.1001

Cited by 9 publications

(10 citation statements)

References 105 publications

(114 reference statements)

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“…Ara h 6 shares secondary and tertiary structure similarity, sequence identity (59%), as well as IgE cross‐reactivity with Ara h 2 (Flinterman et al., ; Koppelman et al., ; Lehmann et al., ). Ara h 6 has a molecular weight of 14.8 kDa and a pI of 5.6 (http://allergen.org; Eigenmann, Burks, Bannon, & Sampson, ; Offermann et al., ). Ara h 6 resembles Ara h 2 in structure sharing a four tightly coiled conformational core helical structure (Figure ), which makes it heat and protease resistant (Sen et al., ).…”

Section: Molecular Characteristics Of Peanut Allergensmentioning

confidence: 99%

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%

Peanut Allergy: Characteristics and Approaches for Mitigation

Shah

Shi

Ashley

et al. 2019

Comp Rev Food Sci Food Safe

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“…33) In terms of Ara h, they are groups of peanut seed allergenic proteins of which biochemical properties (MW and pI) as well as biological roles have been reviewed. 13,42) The three main allergens are Ara h 1 (7S globulin or conarachin), Ara h 3 (11S globulin or arachin), and Ara h 2 (a 2S albumin with trypsin inhibitor activity against pathogen) comprising about 90% of total allergens. 13) These allergens together with another 2S albumin (Ara h 6; a trypsin inhibitor) have been already suggested as protein markers in identification, by SDS-PAGE or 2D-GE, of peanut genotypes at the viewpoint of genotypic markers and nutritional awareness.…”

Section: Discussionmentioning

confidence: 99%

“…The 2S albumins and nsLTPs are also alternatively characterized in the same prolamin superfamily due to conserved cysteine residues and intrachain disulfide bridges similar to the seed storage alcohol-soluble prolamin. 13,42) Most Ara h is soluble in water or saline solution except defensins which could be differently obtained by methanol/ chloroform extraction of peanut seed meal. 13) Regarding to solubility property, these allergens are hardly present in the aqueous ethanolic prolamin fraction from the peanut seeds.…”

Section: Discussionmentioning

confidence: 99%

Identification of peanut seed prolamins with an antifungal role by 2D-GE and drought treatment

Senakoon

Nuchadomrong

Chiou

et al. 2015

Bioscience, Biotechnology, and Biochemistry

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This work revealed peanut seed prolamins likely displaying a defensive role besides the known nitrogen storage. Drought stress and proteomic approaches were used in varieties of peanuts to explore the prolamin member in association with a test against Aspergillus flavus spore germination. The stress effect was showed by aerial biomass, leaf content of malondialdehyde, and seed contamination by A. flavus. Sodium dodecyl sulfate–polyacrylamide gel electrophoresis profiles were not informative for the antifungal polypeptides. From two-dimensional gel electrophoresis, the suspected polypeptides were those with pI 5.45–5.75 and sizes of 22.0–30.5 kDa specifically in Spanish-type peanuts. Regarding to the drought effect in most of these peanuts, the spot peak volume analysis deduced three novel prolamin-related antifungal polypeptides at pI 5.75–5.8 with 30.5, 27.5–28.5, and 22.0–22.5 kDa, which was confirmed after isoelectric purification at pH 5.60. The data could not yet conclude their correlation with resistance to drought and to seed infection by A. flavus.

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“…Peanut is listed among the eight major food allergens ranked by the Food and Agriculture Organization. Peanut allergy is common and typically permanent, moreover, allergy to peanuts and other tree nuts account for the majority of fatal and near-fatal anaphylactic reactions (Celakovska, Ettlerova, Ettler, Vaneckova, & Bukac, 2011;Husain & Schwartz, 2012;Offermann et al, 2015;Peng, Song, Liu, Kuang, & Xu, 2015;Sampson, 2002). At present, 17 peanut allergens are officially registered at the Allergen Nomenclature Sub-Committee of the International Union of Immunological Societies (http://www.allergen.org).…”

Section: Introductionmentioning

confidence: 99%

Analysis on MTGase catalysed cross-linked products of Ara h 2: structure and immunoreactivity

Chang

Zhao

et al. 2018

Food and Agricultural Immunology

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Peanut is ranked among the eight major food allergens. Ara h 2 is its major allergen, recognized by more than 90% of serum IgE from peanut-allergic patients. Cross-linking catalysed by microbial transglutaminase (MTGase) is proved to be feasible to decrease the allergenicity of Ara h 2. The crosslinking reaction occurred both interand intra-molecular could gain products with different molecular weights. In this study, after MTGase catalysed crosslinking, the products were separated into low molecular weight part of Ara h 2 (LP-Ara h 2) and high molecular weight part of Ara h 2 (HP-Ara h 2), and the structure, digestibility, IgG and IgE binding capability of each part were analysed. Compared with LP-Ara h 2, HP-Ara h 2 was found to have looser structure, higher digestion rate and corresponding lower immunogenicity. By controlling the reaction condition to get different products, the protein desensitization processes would get a better result.

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Structural Biology of Peanut Allergens

Cited by 9 publications

References 105 publications

Peanut Allergy: Characteristics and Approaches for Mitigation

Peanut Allergy: Characteristics and Approaches for Mitigation

Identification of peanut seed prolamins with an antifungal role by 2D-GE and drought treatment

Analysis on MTGase catalysed cross-linked products of Ara h 2: structure and immunoreactivity

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