Division of the major birch pollen allergen, Bet v 1, into two non-anaphylactic fragments.
We have expressed in Escherichia coli two halves of the major birch pollen allergen, Bet v 1. Both fragments representing the complete 17-kD allergen were purified to homogeneity. In contrast to the complete recombinant, Bet v 1, the fragments had almost completely lost their IgE-binding capacity and exhibited a random coil structure as analyzed by circular dichroism. The ability of the recombinant fragments to trigger histamine release from allergic patients' basophils as well as their capacity to elicit skin reactions were also largely abolished. Both non-anaphylactic Bet v 1 fragments carried the majority of T cell epitopes and may therefore be considered as safe tools for immunotherapy of tree pollen and associated food allergy.
Vrtala
S
S
Department of Immunopathology, Institute of General and Experimental Pathology, AKH, University of Vienna, Austria.
Hirtenlehner
K
K
Vangelista
L
L
Pastore
A
A
Eichler
H G
HG
Sperr
W R
WR
Valent
P
P
Ebner
C
C
Kraft
D
D
Valenta
R
R
D000485:Allergens / Q000276:immunology*; D052179:Antigens, Plant; D006801:Humans; D007073:Immunoglobulin E / Q000276:immunology; D010446:Peptide Fragments / Q000276:immunology*; D010940:Plant Proteins / Q000276:immunology*; D011994:Recombinant Proteins / Q000276:immunology; D013601:T-Lymphocytes / Q000276:immunology
D000485:Allergens; D052179:Antigens, Plant; D010446:Peptide Fragments; D010940:Plant Proteins; D011994:Recombinant Proteins; C061312:Bet v 1 allergen, Betula; D007073:Immunoglobulin E