Primary sequence and site‐selective hydroxylation of prolines in isoforms of a major peanut allergen protein Ara h 2

Li, Jinxi; Shefcheck, Kevin J.; Callahan, John H.; Fenselau, Catherine

doi:10.1002/pro.295

Cited by 44 publications

(48 citation statements)

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“…Furthermore, Li et al [50] did not find the N-glycosylation site occupied by oligosaccharides, which is in contrast with previous reports [51] . As experimentally shown, Ara h 2 possesses trypsin inhibitor properties [52] .…”

Section: Ara H 2 Ara H 6 and Ara Hcontrasting

confidence: 65%

“…These isoallergens may be generated by amino acid deletion at the C-terminus or amino acid exchanges or site-selective hydroxylation of prolines in positions 46, 53 and 65, as shown by tandem mass spectrometry [50] . Furthermore, Li et al [50] did not find the N-glycosylation site occupied by oligosaccharides, which is in contrast with previous reports [51] .…”

Section: Ara H 2 Ara H 6 and Ara Hmentioning

confidence: 99%

“…Anchor points for disulfide bridges ↶ ↷ may be inverted[50,54]. x represents any amino acid residue.…”

mentioning

confidence: 99%

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Peanut Allergens

Becker

Jappe

2014

Chemical Immunology and Allergy

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The earliest known evidence of peanut farming dates back 7,600 years. With a prevalence of roughly 1%, peanut allergy is a diagnostic and treatment challenge, but is also a very good model for studying all aspects of food allergy, including its molecular basis and pathomechanisms. Therefore, the very starting point for elucidating all these aspects is the identification of peanut allergens with subsequent clearing of their structure and their preparation as pure recombinant and/or natural allergens. This is the basis for in vitro diagnostic tests as well as the development of immunotherapeutic drugs. With regard to class I food allergy, peanut allergy affects by far the largest group of patients. In peanuts, 12 allergens have been identified and their molecular characteristics are described herein. Ara h 1, Ara h 3.01 and Ara h 3.02 (the former Ara h 4) belong to the cupin superfamily. The conglutins Ara h 2, Ara h 6 and Ara h 7, and the non-specific lipid transfer protein Ara h 9 belong to the prolamin superfamily. Ara h 5 (profilin) and Ara h 8 (Bet v 1-homologous protein) cause class II food allergies and are associated with inhalation allergy to pollen via the sequential and/or conformational similarity of molecules. Two peanut oleosins are listed as Ara h 10 and Ara h 11 and two defensins as Ara h 12 and Ara h 13 by the WHO/IUIS Allergen Nomenclature Subcommittee. The effect of the above-specified allergens has to be considered in the context of their matrix, which is influenced by processing factors and the individual's immune system.

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Section: Ara H 2 Ara H 6 and Ara Hcontrasting

confidence: 65%

Section: Ara H 2 Ara H 6 and Ara Hmentioning

confidence: 99%

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Peanut Allergens

Becker

Jappe

2014

Chemical Immunology and Allergy

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“…7). This lack of recognition may be of consequence for the newly emerging component-resolved diagnostic methods that rely on the use of recombinant allergens, and may be explained by the lack of a carbohydrate component of the allergen (60) or by the presence of modified amino acids that have been shown to be present in food proteins, including peanut allergens (61). This difference in the interaction with IgE indicates that the recombinant aller- gen may not always be an adequate replacement of the natural protein in allergy diagnostics.…”

Section: Discussionmentioning

confidence: 99%

Structural and Immunologic Characterization of Ara h 1, a Major Peanut Allergen

Chruszcz

Maleki

Majorek

et al. 2011

Journal of Biological Chemistry

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Allergic reactions to peanuts and tree nuts are major causes of anaphylaxis in the United States. We compare different properties of natural and recombinant versions of Ara h 1, a major peanut allergen, through structural, immunologic, and bioinformatics analyses. Small angle x-ray scattering studies show that natural Ara h 1 forms higher molecular weight aggregates in solution. In contrast, the full-length recombinant protein is partially unfolded and exists as a monomer. The crystal structure of the Ara h 1 core (residues 170 -586) shows that the central part of the allergen has a bicupin fold, which is in agreement with our bioinformatics analysis. In its crystalline state, the core region of Ara h 1 forms trimeric assemblies, while in solution the protein exists as higher molecular weight assemblies. This finding reveals that the residues forming the core region of the protein are sufficient for formation of Ara h 1 trimers and higher order oligomers. Natural and recombinant variants of proteins tested in in vitro gastric and duodenal digestion assays show that the natural protein is the most stable form, followed by the recombinant Ara h 1 core fragment and the full-length recombinant protein. Additionally, IgE binding studies reveal that the natural and recombinant allergens have different patterns of interaction with IgE antibodies. The molecular basis of cross-reactivity between vicilin allergens is also elucidated.

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“…Ara h 2.0201 contains an insertion of 12 amino acids in the hypervariable region containing the immunodominant IgE epitope [67]. The molecular masses of the two isoforms determined by mass spectrometric analysis correspond to the molecular weights calculated from the encoding genes [68], suggesting that Ara h 2 is not glycosylated as previously reported [65]. Among ten identified linear IgE-binding epitopes, three were immunodominant and located in the exposed and structurally flexible regions in the folded protein [69].…”

Section: Allergenic Peanut Prolaminsmentioning

confidence: 99%

Cross-Reactivity of Peanut Allergens

Bublin

Breiteneder

2014

Curr Allergy Asthma Rep

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Peanut seeds are currently widely used as source of human food ingredients in the United States of America and in European countries due to their high quality protein and oil content. This article describes the classification and molecular biology of peanut seed allergens with particular reference to their cross-reactivities. Currently, the IUIS allergen nomenclature subcommittee accepts 12 peanut allergens. Two allergens belong to the cupin and four to the prolamin superfamily, and six are distributed among profilins, Bet v 1-like proteins, oleosins, and defensins. Clinical observations frequently report an association of peanut allergy with allergies to legumes, tree nuts, seeds, fruits and pollen. Molecular cross-reactivity has been described between members of the Bet v 1-like proteins, the non-specific lipid transfer proteins, and the profilins. This review also addresses the less well-studied cross-reactivity between cupin and prolamin allergens of peanuts and of other plant food sources and the recently discovered cross-reactivity between peanut allergens of unrelated protein families.

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Primary sequence and site‐selective hydroxylation of prolines in isoforms of a major peanut allergen protein Ara h 2

Cited by 44 publications

References 10 publications

Peanut Allergens

Peanut Allergens

Structural and Immunologic Characterization of Ara h 1, a Major Peanut Allergen

Cross-Reactivity of Peanut Allergens

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