Immunoglobulin E Binding Reactivity of a Recombinant Allergen Homologous to -Tubulin from Tyrophagus putrescentiae
نویسندگان
چکیده
Immunoglobulin E Binding Reactivity of a Recombinant Allergen Homologous to -Tubulin from Tyrophagus putrescentiae Kyoung Yong Jeong, Haeseok Lee, Jae Sik Lee, Jongweon Lee, In-Yong Lee, Han-Il Ree, Chein-Soo Hong, Jung Won Park, and Tai-Soon Yong* Department of Parasitology and Institute of Tropical Medicine and Department of Internal Medicine and Institute of Allergy, Brain Korea 21 Project for Medical Science, Yonsei University College of Medicine, Seoul, Korea
منابع مشابه
Immunoglobulin E binding reactivity of a recombinant allergen homologous to alpha-Tubulin from Tyrophagus putrescentiae.
Storage mites may cause allergic respiratory diseases in urban areas as well as pose an occupational hazard in rural areas. Characterization of storage mite allergens is important for the development of diagnostic and therapeutic agents against mite-associated allergic disorders. Here we report on the cloning and expression of alpha-tubulin from the storage mite (Tyrophagus putrescentiae). The ...
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BACKGROUND Dust mites are important inducers of allergic disease. Group 2 allergens are recognized as major allergens in several mite species, including Dermatophagoides pteronyssinus, Lepidoglyphus destructor, and Tyrophagus putrescentiae. No allergens have thus far been characterized on the molecular level from the dust mite Glycyphagus domesticus. OBJECTIVE We sought to examine the cross-r...
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Group-5 and group-21 allergens, produced by house dust mites and storage mites are 36.6-55.8% identical in their sequences and are recognized by at least 50% of immunoglobulin (Ig)E from the sera of individuals allergic to dust mites. In the present study, recombinant group-5 and ‑21 allergens from three mite species, Dermatophagoides farinae (rDer f 5 and 21), Tyrophagus putrescentiae (rTyr p ...
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