Immunoglobulin E binding reactivity of a recombinant allergen homologous to α-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 α-tubulin from the storage mite (Tyrophagus putrescentiae). The deduced amino acid sequence of the α-tubulin from the storage mite showed as much as 97.3% identity to the α-tubulin sequences from other organisms. The highly conserved amino acid sequences of α-tubulins across different species of mites may indicate that cross-reactivity for this potential allergen exists. The frequency of immunoglobulin E reactivity of this recombinant protein is 29.3% in sera from storage mite-allergic subjects.