Abstract
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.
| Original language | English |
|---|---|
| Pages (from-to) | 1673-1681 |
| Number of pages | 9 |
| Journal | Journal of Clinical Investigation |
| Volume | 99 |
| Issue number | 7 |
| Publication status | Published - Apr 1 1997 |
| Externally published | Yes |
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Keywords
- Bet v 1
- histamine release
- major birch pollen allergen
- recombinant allergen fragments
- skin testing
ASJC Scopus subject areas
- Medicine(all)
Cite this
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. / Vrtala, Susanne; Hirtenlehner, Kora; Vangelista, Luca; Pastore, Annalisa; Eichler, Hans Georg; Sperr, Wolfgang R.; Valent, Peter; Ebner, Christof; Kraft, Dietrich; Valenta, Rudolf.
In: Journal of Clinical Investigation, Vol. 99, No. 7, 01.04.1997, p. 1673-1681.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - 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
AU - Vrtala, Susanne
AU - Hirtenlehner, Kora
AU - Vangelista, Luca
AU - Pastore, Annalisa
AU - Eichler, Hans Georg
AU - Sperr, Wolfgang R.
AU - Valent, Peter
AU - Ebner, Christof
AU - Kraft, Dietrich
AU - Valenta, Rudolf
PY - 1997/4/1
Y1 - 1997/4/1
N2 - 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.
AB - 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.
KW - Bet v 1
KW - histamine release
KW - major birch pollen allergen
KW - recombinant allergen fragments
KW - skin testing
UR - http://www.scopus.com/inward/record.url?scp=0030937231&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0030937231&partnerID=8YFLogxK
M3 - Article
VL - 99
SP - 1673
EP - 1681
JO - Journal of Clinical Investigation
JF - Journal of Clinical Investigation
SN - 0021-9738
IS - 7
ER -