cDNA Cloning and Protein Analysis of a Bovine Dermal Allergen with Homology to Psoriasin

• Published in: Journal of investigative dermatology Vol. 105; no. 5; pp. 660 - 663
• Main Authors: Rautiainen, Jaakko, Rythönen, Marja, Parkkinen, Sinikka, Pentikäinen, Jaana, Linnala-Kankkunen, Annikka, Virtanen, Tuomas, Pelkonen, Jukka, Mäntyjärvi, Rauno
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 01.11.1995
• Subjects: Allergens - chemistry; Allergens - immunology; Amino Acid Sequence; Animals; Base Sequence; Calcium-Binding Proteins - chemistry; Calcium-Binding Proteins - genetics; Cattle; Cloning, Molecular; DNA, Complementary - genetics; Epitopes - analysis; Gene Expression; Humans; Molecular Sequence Data; Protein Structure, Secondary; S100 Calcium Binding Protein A7; S100 Proteins; Sequence Homology, Amino Acid; Skin - immunology
• ISSN: 0022-202X; 1523-1747
• DOI: 10.1111/1523-1747.ep12324309

Immunoscreening of a cDNA library from bovine skin led to isolation of clones coding for an allergen named BDA11. Sequence analysis of the clones revealed that they can encode a protein of 11.6 kDa with a predicted p1 of 5.19. Allergenicity of BDA11 was verified by the IgE reactivity in cattle-allergic patients' sera with the recombinant protein produced in Escherichia coli. A biochemically purified native allergen of 11 kDa from bovine dander was identified as BDA11 by peptide sequencing. Homology comparisons showed that BDA11 had a 63.4% amino acid identity with human psoriasin. Psoriasin is a calcium-binding protein expressed in keratinocytes, and it is strongly up-regulated in psoriatic skin. BDA11 also had segments homologous with calcium-binding proteins from three other species.