Bip 1, a Monoclonal Antibody with Specificity for the Major Birch Pollen Allergen Bet v 1, Modulates IgE Binding to the Allergen

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منابع مشابه

Trimolecular complex between major birch pollen allergen, Bet v 1, monoclonal allergen-specific human IgE and recombinant CD23

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NMR resonance assignments of a hypoallergenic isoform of the major birch pollen allergen Bet v 1

In Northern America and Europe a great number of people are suffering from birch pollen allergy and pollen related food allergies. The trigger for these immunological reactions is the 17.5 kDa major birch pollen allergen Bet v 1, which belongs to the family of PR-10 (pathogenesis-related) proteins. In nature, Bet v 1 occurs as a mixture of various isoforms that possess different immunological p...

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Ligand Recognition of the Major Birch Pollen Allergen Bet v 1 is Isoform Dependent

Each spring millions of patients suffer from allergies when birch pollen is released into the air. In most cases, the major pollen allergen Bet v 1 is the elicitor of the allergy symptoms. Bet v 1 comes in a variety of isoforms that share virtually identical conformations, but their relative concentrations are plant-specific. Glycosylated flavonoids, such as quercetin-3-O-sophoroside, are the p...

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Crystallographically Mapped Ligand Binding Differs in High and Low IgE Binding Isoforms of Birch Pollen Allergen Bet v 1

The ability of pathogenesis-related proteins of family 10 to bind a broad spectrum of ligands is considered to play a key role for their physiological and pathological functions. In particular, Bet v 1, an archetypical allergen from birch pollen, is described as a highly promiscuous ligand acceptor. However, the detailed recognition mechanisms, including specificity factors discriminating bindi...

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Dominating IgE-binding epitope of Bet v 1, the major allergen of birch pollen, characterized by X-ray crystallography and site-directed mutagenesis.

Specific allergy vaccination is an efficient treatment for allergic disease; however, the development of safer vaccines would enable a more general use of the treatment. Determination of molecular structures of allergens and allergen-Ab complexes facilitates epitope mapping and enables a rational approach to the engineering of allergen molecules with reduced IgE binding. In this study, we descr...

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ژورنال

عنوان ژورنال: International Archives of Allergy and Immunology

سال: 1997

ISSN: 1018-2438,1423-0097

DOI: 10.1159/000237565