cDNA cloning and protein analysis of a bovine dermal allergen with homology to psoriasin

J Invest Dermatol. 1995 Nov;105(5):660-3. doi: 10.1111/1523-1747.ep12324309.

Abstract

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 pI 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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 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*

Substances

  • Allergens
  • Calcium-Binding Proteins
  • DNA, Complementary
  • Epitopes
  • S100 Calcium Binding Protein A7
  • S100 Proteins
  • S100A7 protein, human

Associated data

  • GENBANK/L39834