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Der f 35: An MD ‐2‐like house dust mite allergen that cross‐reacts with Der f 2 and Pso o 2
Author(s) -
Fujimura T.,
Aki T.,
Isobe T.,
Matsuoka A.,
Hayashi T.,
Ono K.,
Kawamoto S.
Publication year - 2017
Publication title -
allergy
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.363
H-Index - 173
eISSN - 1398-9995
pISSN - 0105-4538
DOI - 10.1111/all.13192
Subject(s) - allergen , house dust mite , immunoglobulin e , recombinant dna , mite , allergy , chemistry , immunology , cross reactivity , microbiology and biotechnology , antibody , biology , biochemistry , cross reactions , gene , botany
Background Dermatophagoides farinae is a source of airborne house dust mite ( HDM ) allergens. We elucidated IgE‐reactive allergens from D. farinae by two‐dimensional immunoblotting‐based allergenome analysis, and identified one new allergen, named Der f 35, that possesses IgE‐binding capacity comparable to that of Der f 2. The aim of this study was to clarify the allergenic capacity of new HDM allergen Der f 35. Methods We cloned der f 35 from D. farinae mRNA and produced recombinant Der f 35 in Escherichia coli . The IgE‐binding capacity of Der f 35 and its cross‐reactivity with group 2 allergens from D. farinae and Psoroptes ovis were determined by enzyme‐linked immunosorbent assay (ELISA) and ELISA inhibition assays, respectively. Results The deduced amino acid sequence for der f 35 , which possesses the MD ‐2‐related lipid‐recognition domain, showed higher identity with group 2 allergens from P. ovis (61.5%) and Blomia tropicalis (50.7%) than with Der f 2 (40.8%). Der f 35 showed IgE‐binding frequencies of 77.5% (31/40) for the native form upon allergenome analysis and 51.4% (18/35) for recombinant structure by ELISA . Der f 35 showed cross‐reactivity with Der f 2 and Pso o 2 in reaction with HDM ‐allergic patients' IgE by ELISA inhibition assay. Conclusion Der f 35 is a candidate major allergen from D. farinae , which is more similar to group 2 allergens from sheep scab mite and storage mites. Der f 35 could be responsible for the cross‐reactivity among group 2 mite allergens.