Animal-derived food allergen: A review on the available crystal structure and new insights into structural epitope.

Publisher: Institute of Food Technologists Country of Publication: United States NLM ID: 101305205 Publication Model: Print Cited Medium: Internet ISSN: 1541-4337 (Electronic) Linking ISSN: 15414337 NLM ISO Abbreviation: Compr Rev Food Sci Food Saf Subsets: MEDLINE

Original Publication: Chicago, Ill. : Institute of Food Technologists

Allergens*/chemistry ; Allergens*/immunology ; Food Hypersensitivity*/immunology ; Epitopes*/chemistry ; Epitopes*/immunology ; Immunoglobulin E*/immunology ; Immunoglobulin E*/chemistry; Animals ; Crystallography, X-Ray ; Humans ; Cross Reactions ; Protein Conformation

Immunoglobulin E (IgE)-mediated food allergy is a rapidly growing public health problem. The interaction between allergens and IgE is at the core of the allergic response. One of the best ways to understand this interaction is through structural characterization. This review focuses on animal-derived food allergens, overviews allergen structures determined by X-ray crystallography, presents an update on IgE conformational epitopes, and explores the structural features of these epitopes. The structural determinants of allergenicity and cross-reactivity are also discussed. Animal-derived food allergens are classified into limited protein families according to structural features, with the calcium-binding protein and actin-binding protein families dominating. Progress in epitope characterization has provided useful information on the structural properties of the IgE recognition region. The data reveals that epitopes are located in relatively protruding areas with negative surface electrostatic potential. Ligand binding and disulfide bonds are two intrinsic characteristics that influence protein structure and impact allergenicity. Shared structures, local motifs, and shared epitopes are factors that lead to cross-reactivity. The structural properties of epitope regions and structural determinants of allergenicity and cross-reactivity may provide directions for the prevention, diagnosis, and treatment of food allergies. Experimentally determined structure, especially that of antigen-antibody complexes, remains limited, and the identification of epitopes continues to be a bottleneck in the study of animal-derived food allergens. A combination of traditional immunological techniques and emerging bioinformatics technology will revolutionize how protein interactions are characterized.
(© 2024 Institute of Food Technologists®.)

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2023J011666 The Grant from the Provincial Natural Scientific Foundation of Fujian Province; 31901811 National Natural Scientific Foundation of China; 32072336 National Natural Scientific Foundation of China; 32001695 National Natural Scientific Foundation of China; 2022YFF1100103 The National Key R&D Program of China; HX201808 the Financial Support of Scientific Research Foundation of Xiamen Huaxia University

Keywords: animal‐derived food allergen; conformational epitope; cross‐reactivity; crystal structure; protein family

0 (Allergens)
0 (Epitopes)
37341-29-0 (Immunoglobulin E)

Date Created: 20240523 Date Completed: 20240523 Latest Revision: 20240523

20240524

10.1111/1541-4337.13340

38778570