Before insects can be used widely as an alternative source of dietary protein, their allerginicity should be investigated. Therefore, the aim of our study was to assess the potential adverse reactions of the immune system of dogs against Tenebrio molitor proteins. Dogs sensitised to storage mites T. putrescentiae and A. siro were included. Clinically healthy and clinically allergic dogs were compared. Proteins were extracted from mealworm larvae and their digestibility determined by in vitro incubation with digestive proteases. Mealworm protein extracts and digests were analysed by SDS-PAGE. Canine sera tested for the presence of mite-specific IgEs were used for subsequent Western blotting. LC-MS/MS analysis was used to identify mealworm proteins and their allergenic potential was predicted with the AllermatchTM tool. The binding of canine sera IgEs to mealworm proteins was confirmed; however, the differences between the two groups of dogs were not significant. Moreover, no clear correlation was found between sensitisation to storage mites and clinical status of the dogs. Altogether, 17 different proteins were identified, including tropomyosin, α-amylase, and Tm-E1a cuticular protein that are known cross-reacting IgE-binding allergens. Our results suggest that dogs allergic to mites may clinically express also the cross-reactivity with mealworm proteins.
Keywords: allergy; dogs; mealworm; mites; proteomics.