
Food allergies originate from adverse immune reactions to some food components. Ingestion of food allergens can cause effects of varying severity, from mild itching to severe anaphylaxis reactions. Currently there are no clues to predict the allergenic potency of a molecule, nor are cures for food allergies available. Cutting-edge research on allergens is aimed at increasing information on their diffusion and understanding structure-allergenicity relationships. In this context, purified recombinant allergens are valuable tools for advances in the diagnostic and immunotherapeutic fields. Chitinases are a group of allergens often found in plant fruits, but also identified in edible insects. They are classified into different families and classes for which structural analyses and identification of epitopes have been only partially carried out. Moreover, also their presence in common allergen databases is not complete. In this review we provide a summary of the identified food allergenic chitinases, their main structural characteristics, and a clear division in the different classes.
food allergy, Insecta, Chitinases, Organic chemistry, Review, Allergens, Cross Reactions, Immunoglobulin E, epitope mapping, Epitopes, Structure-Activity Relationship, QD241-441, chitinase, Animals, Humans, Epitope Mapping, Food Hypersensitivity, allergen, Plant Proteins
food allergy, Insecta, Chitinases, Organic chemistry, Review, Allergens, Cross Reactions, Immunoglobulin E, epitope mapping, Epitopes, Structure-Activity Relationship, QD241-441, chitinase, Animals, Humans, Epitope Mapping, Food Hypersensitivity, allergen, Plant Proteins
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