Purification, characterization and N-terminal amino acid sequence of a new major allergen from European chestnut pollen--Cas s 1

Biochem Biophys Res Commun. 1993 Nov 15;196(3):1086-92. doi: 10.1006/bbrc.1993.2362.

Abstract

Pollens from trees of the order Fagales (e.g. birch, alder, hazel, and hornbeam) all contain one major allergen--the main cause for tree pollen allergy. So far the major allergens from birch (Bet v 1), alder (Aln g 1), hazel (Cor a 1), and hornbeam (Car b 1) have been characterized, showing high sequence similarity with each other (1-4). We present the molecular and immunologic characterization of Cas s 1, the major allergen from the European chestnut (Castanea sativa). From aqueous pollen extracts from European chestnut a protein was purified to homogeneity and was subjected to further investigation. The protein revealed a Mr of 22 kDa and was shown to represent the major allergen of the European chestnut (immunoblotting, histamine release) and designated Cas s 1. Despite a marked difference in Mr, Cas s 1 shows significant amino acid sequence similarity at the N-terminus and is antigenically closely related to the major birch pollen allergen Bet v 1 (17 kDa), as shown by binding to the anti-Bet v 1 monoclonal antibody BIP-1 and by IgE-inhibition tests using recombinant Bet v 1.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Allergens / chemistry*
  • Allergens / immunology
  • Allergens / isolation & purification
  • Amino Acid Sequence
  • Antibodies / blood
  • Antibodies, Monoclonal
  • Electrophoresis, Polyacrylamide Gel
  • Europe
  • Histamine Release
  • Humans
  • Immunoblotting
  • Molecular Sequence Data
  • Reference Values
  • Rhinitis, Allergic, Seasonal / blood
  • Rhinitis, Allergic, Seasonal / immunology
  • Sequence Homology, Amino Acid
  • Trees*

Substances

  • Allergens
  • Antibodies
  • Antibodies, Monoclonal