Identification of cross-reactive allergens between the Dermatophagoides farinae house dust mite and the Toxocara canis nematode in dogs with suspected allergies

BACKGROUND: Immunoglobulin (Ig)E cross-reactivity has been shown between Dermatophagoides farinae (Df; house dust mite) and the nematode Toxocara canis (Tc), yet its allergen basis is unknown. OBJECTIVES: To identify the Df allergens IgE-cross-reactive with those of Tc. ANIMALS: Archived sera from 73 dogs with suspected allergy sensitised to Df. MATERIALS AND METHODS: We performed a combination of Pet Allergy Xplorer (PAX) and enzyme-linked immunosorbent assay (ELISA) inhibitions with excretory-secretory and somatic (i.e. nematode body) extracts of Tc or recombinant Tc tropomyosin on coats of Df, Der f 15 and Zen-1 (ELISA) or PAX allergens. RESULTS: The ELISA and PAX inhibitions established that there is mutual yet variable cross-reactivity between the Tc excretory-secretory extract, purified Der f 15 and purified Zen-1. This cross-reactivity is likely to involve cross-reactive glycans, as there is no inhibition between the Tc excretory-secretory extract and recombinant Der f 15 without its predicted natural O-glycans. We also confirmed a heterogeneous cross-reactivity between the somatic Tc extract and Der p 11 (paramyosin), as well as between the recombinant Toxo c 3 and Der p 10 tropomyosins. The cross-reactivity among tropomyosins and paramyosins is likely to involve peptidic epitopes, as these recombinant allergens are not glycosylated. CONCLUSIONS AND CLINICAL RELEVANCE: In dogs with suspected allergies, the cross-reactivity between Tc and Df for dogs is complex and heterogeneous. Some of the cross-reactive IgE recognises shared glycans on Der f 15 and Zen-1, while some targets peptidic epitopes on shared paramyosins and tropomyosins. We do not exclude that additional cross-reactive allergens between Df and Tc also might exist.

Authors: T. Olivry, A. Mas-Fontao, S. Jacquenet, M. Aumayr, T. Tsukui, V. Gomord, L. Faye and C. Favrot Title: Identification of cross-reactive allergens between the Dermatophagoides farinae house dust mite and the Toxocara canis nematode in dogs with suspected allergies Full source: Vet Dermatol, 2024,Vol 35, Iss 6, pp 662-671
Résumé, analyse et commentaires
Aucun.
Photo
Aucune.
Analysis
None.
Abstract	Source
BACKGROUND: Immunoglobulin (Ig)E cross-reactivity has been shown between Dermatophagoides farinae (Df; house dust mite) and the nematode Toxocara canis (Tc), yet its allergen basis is unknown. OBJECTIVES: To identify the Df allergens IgE-cross-reactive with those of Tc. ANIMALS: Archived sera from 73 dogs with suspected allergy sensitised to Df. MATERIALS AND METHODS: We performed a combination of Pet Allergy Xplorer (PAX) and enzyme-linked immunosorbent assay (ELISA) inhibitions with excretory-secretory and somatic (i.e. nematode body) extracts of Tc or recombinant Tc tropomyosin on coats of Df, Der f 15 and Zen-1 (ELISA) or PAX allergens. RESULTS: The ELISA and PAX inhibitions established that there is mutual yet variable cross-reactivity between the Tc excretory-secretory extract, purified Der f 15 and purified Zen-1. This cross-reactivity is likely to involve cross-reactive glycans, as there is no inhibition between the Tc excretory-secretory extract and recombinant Der f 15 without its predicted natural O-glycans. We also confirmed a heterogeneous cross-reactivity between the somatic Tc extract and Der p 11 (paramyosin), as well as between the recombinant Toxo c 3 and Der p 10 tropomyosins. The cross-reactivity among tropomyosins and paramyosins is likely to involve peptidic epitopes, as these recombinant allergens are not glycosylated. CONCLUSIONS AND CLINICAL RELEVANCE: In dogs with suspected allergies, the cross-reactivity between Tc and Df for dogs is complex and heterogeneous. Some of the cross-reactive IgE recognises shared glycans on Der f 15 and Zen-1, while some targets peptidic epitopes on shared paramyosins and tropomyosins. We do not exclude that additional cross-reactive allergens between Df and Tc also might exist.