Immunologic characterization of monoclonal antibodies that modulate human IgE binding to the major birch pollen allergen Bet v 1.
BACKGROUND: Bet v 1 and homologous proteins represent major allergens for almost 95% of patients allergic to tree pollen and approximately 70% of those allergic to fruits and vegetables. As yet, no continuous (sequential) IgE epitopes have been determined for Bet v 1, and evidence has accumulated t...
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| Fformat: | Journal article |
| Iaith: | English |
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1997
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| author | Lebecque, S Dolecek, C Laffer, S Visco, V Denépoux, S Pin, J Guret, C Boltz-Nitulescu, G Weyer, A Valenta, R |
| author_facet | Lebecque, S Dolecek, C Laffer, S Visco, V Denépoux, S Pin, J Guret, C Boltz-Nitulescu, G Weyer, A Valenta, R |
| author_sort | Lebecque, S |
| collection | OXFORD |
| description | BACKGROUND: Bet v 1 and homologous proteins represent major allergens for almost 95% of patients allergic to tree pollen and approximately 70% of those allergic to fruits and vegetables. As yet, no continuous (sequential) IgE epitopes have been determined for Bet v 1, and evidence has accumulated that Bet v 1 IgE epitopes belong to the conformational (discontinuous) type. OBJECTIVE: A panel of 85 mouse monoclonal anti-Bet v 1 antibodies was raised as a tool with which to study the interaction of human IgE antibodies with Bet v 1. METHODS: The epitopes of selected monoclonal antibodies (mAbs) were characterized by mapping with synthetic overlapping peptides and by cross-competition experiments. Cross-reactivity of Bet v 1-specific mAbs with tree and plant food allergens was investigated by Western blotting. The influence of Bet v 1-specific mAbs on the IgE-Bet v 1 interaction was studied by competition assays with immobilized purified recombinant Bet v 1 and by basophil histamine release experiments. RESULTS: Antibodies that increased the IgE binding to Bet v 1 up to fivefold could be defined, whereas others inhibited IgE binding to Bet v 1 up to 99% and competed with the Bet v 1-induced histamine release from patients' basophils. CONCLUSION: The activity of the enhancing antibodies is interpreted as a stabilization of Bet v 1 states/IgE epitopes, which are either more accessible for certain IgE antibodies or are recognized with higher affinity. Those mAbs that competed with the Bet v 1-IgE interaction, if humanized or produced as recombinant antibody fragments, might be considered as potential tools for local allergy therapy. |
| first_indexed | 2024-03-06T19:17:11Z |
| format | Journal article |
| id | oxford-uuid:18ce9ce6-dbc6-415a-a17c-87b83a807947 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T19:17:11Z |
| publishDate | 1997 |
| record_format | dspace |
| spelling | oxford-uuid:18ce9ce6-dbc6-415a-a17c-87b83a8079472022-03-26T10:45:16ZImmunologic characterization of monoclonal antibodies that modulate human IgE binding to the major birch pollen allergen Bet v 1.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:18ce9ce6-dbc6-415a-a17c-87b83a807947EnglishSymplectic Elements at Oxford1997Lebecque, SDolecek, CLaffer, SVisco, VDenépoux, SPin, JGuret, CBoltz-Nitulescu, GWeyer, AValenta, R BACKGROUND: Bet v 1 and homologous proteins represent major allergens for almost 95% of patients allergic to tree pollen and approximately 70% of those allergic to fruits and vegetables. As yet, no continuous (sequential) IgE epitopes have been determined for Bet v 1, and evidence has accumulated that Bet v 1 IgE epitopes belong to the conformational (discontinuous) type. OBJECTIVE: A panel of 85 mouse monoclonal anti-Bet v 1 antibodies was raised as a tool with which to study the interaction of human IgE antibodies with Bet v 1. METHODS: The epitopes of selected monoclonal antibodies (mAbs) were characterized by mapping with synthetic overlapping peptides and by cross-competition experiments. Cross-reactivity of Bet v 1-specific mAbs with tree and plant food allergens was investigated by Western blotting. The influence of Bet v 1-specific mAbs on the IgE-Bet v 1 interaction was studied by competition assays with immobilized purified recombinant Bet v 1 and by basophil histamine release experiments. RESULTS: Antibodies that increased the IgE binding to Bet v 1 up to fivefold could be defined, whereas others inhibited IgE binding to Bet v 1 up to 99% and competed with the Bet v 1-induced histamine release from patients' basophils. CONCLUSION: The activity of the enhancing antibodies is interpreted as a stabilization of Bet v 1 states/IgE epitopes, which are either more accessible for certain IgE antibodies or are recognized with higher affinity. Those mAbs that competed with the Bet v 1-IgE interaction, if humanized or produced as recombinant antibody fragments, might be considered as potential tools for local allergy therapy. |
| spellingShingle | Lebecque, S Dolecek, C Laffer, S Visco, V Denépoux, S Pin, J Guret, C Boltz-Nitulescu, G Weyer, A Valenta, R Immunologic characterization of monoclonal antibodies that modulate human IgE binding to the major birch pollen allergen Bet v 1. |
| title | Immunologic characterization of monoclonal antibodies that modulate human IgE binding to the major birch pollen allergen Bet v 1. |
| title_full | Immunologic characterization of monoclonal antibodies that modulate human IgE binding to the major birch pollen allergen Bet v 1. |
| title_fullStr | Immunologic characterization of monoclonal antibodies that modulate human IgE binding to the major birch pollen allergen Bet v 1. |
| title_full_unstemmed | Immunologic characterization of monoclonal antibodies that modulate human IgE binding to the major birch pollen allergen Bet v 1. |
| title_short | Immunologic characterization of monoclonal antibodies that modulate human IgE binding to the major birch pollen allergen Bet v 1. |
| title_sort | immunologic characterization of monoclonal antibodies that modulate human ige binding to the major birch pollen allergen bet v 1 |
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