Conversion of the major birch pollen allergen, Bet v 1, into two nonanaphylactic T cell epitope-containing fragments: candidates for a novel form of specific immunotherapy

J Clin Invest. 1997 Apr 1;99(7):1673-81. doi: 10.1172/JCI119330.


A novel approach to reduce the anaphylactic activity of allergens is suggested. The strategy makes use of the presence of conformational immunoglobulin E (IgE) epitopes on one of the most common allergens. The three dimensional structure of the major birch pollen allergen, Bet v 1, was disrupted by expressing two parts of the Bet v 1 cDNA representing amino acids 1-74 and 75-160 in Escherichia coli. In contrast to the complete recombinant Bet v 1, the fragments showed almost no allergenicity and exhibited random coil conformation as analyzed by circular dichroism. Both nonanaphylactic fragments induced proliferation of human Bet v 1-specific T cell clones, indicating that they harbored all dominant T cell epitopes and therefore may be considered as a basis for the development of a safe and specific T cell immunotherapy.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Allergens*
  • Anaphylaxis / prevention & control
  • Animals
  • Antigens, Plant
  • Circular Dichroism
  • Epitopes*
  • Histamine Release
  • Humans
  • Hypersensitivity / therapy*
  • Immunoglobulin E / metabolism
  • Immunotherapy
  • Mice
  • Peptide Fragments / immunology*
  • Plant Proteins / chemistry*
  • Plant Proteins / immunology
  • Plant Proteins / isolation & purification
  • Protein Conformation
  • Recombinant Proteins / isolation & purification
  • T-Lymphocytes / immunology*


  • Allergens
  • Antigens, Plant
  • Epitopes
  • Peptide Fragments
  • Plant Proteins
  • Recombinant Proteins
  • Bet v 1 allergen, Betula
  • Immunoglobulin E