HOMOLOGY OF A BOVINE ALLERGEN AND THE OLIGOMYCIN SENSITIVITY-CONFERRING PROTEIN OF THE MITOCHONDRIAL ADENOSINE-TRIPHOSPHATE SYNTHASE COMPLEX

We have characterized bovine allergens by constructing and analyzing a complementary DNA library from bovine skin. Clones producing proteins that reacted with IgE antibodies from persons with allergy were purif ied and sequenced. One set of the allergen-coding clones showed an alm ost complete homology with the bovine oligomycin sensitivity-conferrin g protein of the mitochondrial adenosine triphosphate synthase complex . The IgE antibodies adsorbed with the recombinant allergen reacted wi th an II kd protein in the cow dander extract. Binding of the IgE from patients allergic to the recombinant allergen expressed in Escherichi a coli confirmed the allergen-coding ability of the complementary DNA sequence. The prevalence of the IgE-positive sera among patients with cow allergy and control subjects suggests that the recombinant allerge n represents one of the minor allergens in cow dander. This is the fir st time a mammalian allergen has been identified as a protein with a k nown function.