IgE cross-inhibition between Ara h 1 and Ara h 2 is explained by complex formation of both major peanut allergens

Warmenhoven, Hans; Hulsbos, Luuk; Dreskin, Stephen C.; Akkerdaas, Jaap H.; Versteeg, Serge A.; Ree, Ronald van

doi:10.1016/j.jaci.2023.03.025

Cited by 6 publications

(3 citation statements)

References 43 publications

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“…However, though the co-sensitization between legumes in patient groups allergic to different legumes could be partially attributed to the 2S albumins, and the main allergens responsible for the co-sensitization in other studies were reported to be the 11S and 7S globulins [219]. In addition, IgE cross-reactivities were also reported between peanut allergens Ara h 1, Ara h 2, and Ara h 3 [220], but a recent study suggested the reported cross-reactivities likely resulted from the complex formation of the allergens [221]. Furthermore, IgE crossreactivity between different foods was reported as not always being clinically relevant [219].…”

Section: Cross-reactivitymentioning

confidence: 95%

Food Allergens of Plant Origin

Zhang

Che

et al. 2023

Foods

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This review presents an update on the physical, chemical, and biological properties of food allergens in plant sources, focusing on the few protein families that contribute to multiple food allergens from different species and protein families recently found to contain food allergens. The structures and structural components of the food allergens in the allergen families may provide further directions for discovering new food allergens. Answers as to what makes some food proteins allergens are still elusive. Factors to be considered in mitigating food allergens include the abundance of the protein in a food, the property of short stretches of the sequence of the protein that may constitute linear IgE binding epitopes, the structural properties of the protein, its stability to heat and digestion, the food matrix the protein is in, and the antimicrobial activity to the microbial flora of the human gastrointestinal tract. Additionally, recent data suggest that widely used techniques for mapping linear IgE binding epitopes need to be improved by incorporating positive controls, and methodologies for mapping conformational IgE binding epitopes need to be developed.

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Section: Cross-reactivitymentioning

confidence: 95%

Food Allergens of Plant Origin

Zhang

Che

et al. 2023

Foods

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“… 68 , 69 , 70 , 71 A previous study published in the Journal of Allergy and Clinical Immunology reported immunologic cross-reactivity between the peanut major allergens Ara h 1, Ara h 2, and Ara h 3. 72 Warmenhoven et al 73 recently published evidence that this cross-inhibition between Ara h 1 or Ara h 3 and Ara h 2 was due to formation of complexes between the major allergens and contamination of natural Ara h 1 and Ara h 3 with 2S albumin Ara h 2. For this reason, recombinant allergens are preferred for diagnostics, as cross-contamination with Ara h 2 could lead to overestimation of the clinical relevance of Ara h 1 and Ara h 3 sensitizations.…”

Section: Immune Mechanisms Of Famentioning

confidence: 99%

Feast for thought: A comprehensive review of food allergy 2021-2023

Bartha,

Almulhem,

Santos

2024

Journal of Allergy and Clinical Immunology

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“…Chen et al verified the conformational epitope by mutating the critical amino acid in the conformational epitope predicted by SCP into alanine and observing the changes in the IgG-/IgE-binding capacity of the mutant. It is worth noting that IgE epitopes with conservation properties often cause cross-reactivity, and special IgE epitopes could also serve as biomarkers for detecting allergen components. , The position of IgE epitopes in the tertiary structure determines their IgE-binding capacity . However, only six IgE linear epitopes of the allergenic predominant region of Scy p 9 had been validated, and it is not yet clear whether there are conformational epitopes and other linear epitopes in Scy p 9.…”

Section: Introductionmentioning

confidence: 99%

Immunoglobulin E Epitope Mapping and Structure–Allergenicity Relationship Analysis of Crab Allergen Scy p 9

He,

Yang,

Chen

et al. 2023

J. Agric. Food Chem.

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Filamin C is an allergen of Scylla paramamosain (Scy p 9), and six IgE linear epitopes of the allergenic predominant region had previously been validated. However, the IgE epitope and structure–allergenicity relationship of Scy p 9 are unclear. In this study, a hydrophobic bond was found to be an important factor of conformation maintaining. The critical amino acids in the six predicted conformational epitopes were mutated, and the IgE-binding capacity and surface hydrophobicity of four mutants (E216A, T270A, Y699A, and V704A) were reduced compared to Scy p 9. Ten linear epitopes were verified with synthetic peptides, among which L-AA187–205 had the strongest IgE-binding capacity. In addition, IgE epitopes were mapped in the protruding surface of the tertiary structure, which were conducive to binding with IgE and exhibited high conservation among filamin genes. Overall, these data provided a basis for IgE epitope mapping and structure–allergenicity relationship of Scy p 9.

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IgE cross-inhibition between Ara h 1 and Ara h 2 is explained by complex formation of both major peanut allergens

Cited by 6 publications

References 43 publications

Food Allergens of Plant Origin

Food Allergens of Plant Origin

Feast for thought: A comprehensive review of food allergy 2021-2023

Immunoglobulin E Epitope Mapping and Structure–Allergenicity Relationship Analysis of Crab Allergen Scy p 9

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