Abstract
Bet v 1 and homologous proteins represent major cross-reactive allergens for more than 95% of tree pollen-, fruit-, and vegetable-allergic individuals. To study the interaction of Bet v 1 and the immune system, we characterized a Bet v 1-specific mAb, Bip 1. Soluble rBip 1 Fabs were expressed in Escherichia coli and purified by affinity chromatography using immobilized Bet v 1. Bip 1 Fabs displayed a cross-reactivity to homologous allergens comparable with that of IgE Abs from allergic patients. Preincubation of Bet v 1 with Bip 1 led to an up to fivefold increase of allergic patients' IgE binding to Bet v 1. This enhancement in IgE binding may be interpreted as stabilization of a Bet v 1 state, in which certain IgE epitopes are better applicable. It also shows that allergic patients possess IgE Abs directed against different Bet v 1 conformations. The modulation of Ab binding to a given Ag by other Abs was observed also for human Bet v 1-specific IgG Abs, and may represent a novel mechanism for the regulation of specific humoral immune responses in a complex network.
| Original language | English |
|---|---|
| Pages (from-to) | 4953-4962 |
| Number of pages | 10 |
| Journal | Journal of Immunology |
| Volume | 157 |
| Issue number | 11 |
| Publication status | Published - Dec 1 1996 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Immunology
Cite this
Molecular Characterization of Bip 1, a Monoclonal Antibody That Modulates IgE Binding to Birch Pollen Allergen, Bet v 1. / Laffer, Sylvia; Vangelista, Luca; Steinberger, Peter; Kraft, Dietrich; Pastore, Annalisa; Valenta, Rudolf.
In: Journal of Immunology, Vol. 157, No. 11, 01.12.1996, p. 4953-4962.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Molecular Characterization of Bip 1, a Monoclonal Antibody That Modulates IgE Binding to Birch Pollen Allergen, Bet v 1
AU - Laffer, Sylvia
AU - Vangelista, Luca
AU - Steinberger, Peter
AU - Kraft, Dietrich
AU - Pastore, Annalisa
AU - Valenta, Rudolf
PY - 1996/12/1
Y1 - 1996/12/1
N2 - Bet v 1 and homologous proteins represent major cross-reactive allergens for more than 95% of tree pollen-, fruit-, and vegetable-allergic individuals. To study the interaction of Bet v 1 and the immune system, we characterized a Bet v 1-specific mAb, Bip 1. Soluble rBip 1 Fabs were expressed in Escherichia coli and purified by affinity chromatography using immobilized Bet v 1. Bip 1 Fabs displayed a cross-reactivity to homologous allergens comparable with that of IgE Abs from allergic patients. Preincubation of Bet v 1 with Bip 1 led to an up to fivefold increase of allergic patients' IgE binding to Bet v 1. This enhancement in IgE binding may be interpreted as stabilization of a Bet v 1 state, in which certain IgE epitopes are better applicable. It also shows that allergic patients possess IgE Abs directed against different Bet v 1 conformations. The modulation of Ab binding to a given Ag by other Abs was observed also for human Bet v 1-specific IgG Abs, and may represent a novel mechanism for the regulation of specific humoral immune responses in a complex network.
AB - Bet v 1 and homologous proteins represent major cross-reactive allergens for more than 95% of tree pollen-, fruit-, and vegetable-allergic individuals. To study the interaction of Bet v 1 and the immune system, we characterized a Bet v 1-specific mAb, Bip 1. Soluble rBip 1 Fabs were expressed in Escherichia coli and purified by affinity chromatography using immobilized Bet v 1. Bip 1 Fabs displayed a cross-reactivity to homologous allergens comparable with that of IgE Abs from allergic patients. Preincubation of Bet v 1 with Bip 1 led to an up to fivefold increase of allergic patients' IgE binding to Bet v 1. This enhancement in IgE binding may be interpreted as stabilization of a Bet v 1 state, in which certain IgE epitopes are better applicable. It also shows that allergic patients possess IgE Abs directed against different Bet v 1 conformations. The modulation of Ab binding to a given Ag by other Abs was observed also for human Bet v 1-specific IgG Abs, and may represent a novel mechanism for the regulation of specific humoral immune responses in a complex network.
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M3 - Article
VL - 157
SP - 4953
EP - 4962
JO - Journal of Immunology
JF - Journal of Immunology
SN - 0022-1767
IS - 11
ER -