
doi: 10.1159/000358860
pmid: 24925403
Allergic diseases triggered by mite allergens include allergic rhinoconjunctivitis, asthma, atopic dermatitis and other skin diseases. Since the early discovery of the allergenic role of mites of the genus Dermatophagoides in the mid 1960s, numerous species have been described as the source of allergens capable of sensitizing and inducing allergic symptoms in sensitized and genetically predisposed individuals. The main sources of allergens in house dust worldwide are the fecal pellets of the mite species D. pteronyssinus, D. farinae, Euroglyphus maynei and the storage mites Blomia tropicalis, Lepidoglyphus destructor and Tyropahgus putrescentiae. Group 1 and 2 allergens are major house dust mite allergens. The main allergens in storage mites include fatty acid-binding proteins, tropomyosin and paramyosin homologues, apolipophorin-like proteins, α-tubulins and others, such as group 2, 5 and 7 allergens. Cross-reactivity is an important and common immunological feature among mites. Currently, purified native or recombinant allergens, epitope mapping, proteomic approaches and T cell proliferation techniques are being used to assess cross-reactivity. Mites contain potent enzymes capable of degrading a wide range of substrates. Most mite allergens are enzymes. Advances in genomics and molecular biology will improve our ability to understand the genetics of specific IgE responses to mites. Mite allergen avoidance and immunotherapy are the only two allergen-specific ways to treat mite-induced respiratory and cutaneous diseases.
Mites, Pyroglyphidae, Tropomyosin, Allergens, History, 20th Century, Immunoglobulin E, Fatty Acid-Binding Proteins, Asthma, Tubulin, Hypersensitivity, Animals, Immunotherapy, Protein Binding
Mites, Pyroglyphidae, Tropomyosin, Allergens, History, 20th Century, Immunoglobulin E, Fatty Acid-Binding Proteins, Asthma, Tubulin, Hypersensitivity, Animals, Immunotherapy, Protein Binding
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