Homology of a bovine allergen and the oligomycin sensitivity–conferring protein of the mitochondrial adenosine triphosphate synthase complex

• Published in: Journal of allergy and clinical immunology Vol. 95; no. 6; pp. 1255 - 1260
• Main Authors: Parkkinen, Sinikka, Rytkönen, Marja, Pentikäinen, Jaana, Virtanen, Tuomas, Mäntyjärvi, Rauno
• Format: Journal Article
• Language: English
• Published: New York, NY Mosby, Inc 01.06.1995; Elsevier
• Subjects: Adenosine Triphosphatases - chemistry; Adenosine Triphosphatases - genetics; Adenosine Triphosphatases - isolation & purification; Allergens - chemistry; Allergens - genetics; Allergens - isolation & purification; Allergic diseases; Animals; Base Sequence; Biological and medical sciences; Bovine allergen; Carrier Proteins; Cattle; Cloning, Molecular; complementary DNA cloning; DNA, Complementary - genetics; Escherichia coli - genetics; General aspects; IgE binding; Immunopathology; Medical sciences; Membrane Proteins - chemistry; Membrane Proteins - genetics; Membrane Proteins - isolation & purification; Mitochondria - chemistry; Molecular Sequence Data; oligomycin sensitivity–conferring protein; Sequence Alignment; OSCP; TBS; Bovine allergen; cDNA; IgE binding; complementary DNA cloning; ATP; oligomycin sensitivity–conferring protein; TRIS; Bovine; Enzyme; H; Homology; Dermoskeleton; transporting ATP synthase; Proteins; Vertebrata; Sensitivity; Mammalia; Complementary DNA; Hydrolases; Artiodactyla; Molecular cloning; Ungulata; Allergen
• ISSN: 0091-6749; 1097-6825
• DOI: 10.1016/S0091-6749(95)70083-8

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 purified and sequenced. One set of the allergen-coding clones showed an almost complete homology with the bovine oligomycin sensitivity–conferring protein of the mitochondrial adenosine triphosphate synthase complex. The IgE antibodies adsorbed with the recombinant allergen reacted with an 11 kd protein in the cow dander extract. Binding of the IgE from patients allergic to the recombinant allergen expressed in Escherichia 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 allergen represents one of the minor allergens in cow dander. This is the first time a mammalian allergen has been identified as a protein with a known function. ( J Allergy Clin Immunol 1995;95:1255-60.)