Abstract
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.
Highlights
Food allergies originating from a cross-link reaction between specific food proteins and IgEs represent a serious health concern in everyday life, due to the increasing habits to consume ready-to-eat products
Food allergenic chitinases are a relatively small group of proteins, but their relevance as allergens cannot be underestimated given their presence in highly consumed fruits and plant derivatives
It is necessary to have a clear representation of their diffusion, allergenic potency and structural characteristics
Summary
Food allergies originating from a cross-link reaction between specific food proteins (the allergens) and IgEs (immunoglobulin Es) represent a serious health concern in everyday life, due to the increasing habits to consume ready-to-eat products. The GH18 family comprises about 17,800 chitinases, including about 13,600 of bacterial origin, 3500 from eukaryotes and 300 from viruses They are characterized by a signal peptide and a conserved (β/α) structure containing the catalytic module. Its detection deserves particular interest since silkworm pupae are a traditional food in East Asia, which can be of possible development as a new food habit in other countries For both plant and insect chitinases the possibility that the allergic reaction is due to the so-called cross-reactivity syndrome, i.e., the onset of food allergy in subjects already exposed and sensitized to structurally similar non food allergens, can be considered. In the Molecule column, I stands for allergens identified on the basis of partial sequencing (or mass spectrometry analysis); P indicates allergens purified from the food source; R corresponds to allergens available as recombinant proteins. These molecules, do not show the chitin binding module and should be considered as class II chitinases
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