Birch (Betula verrucosa) pollen-associated food allergy is a well-characterized syndrome, which is due to the cross-reactivity of IgE antibodies to homologous allergens in various foods. One crossreacting area on the major birch pollen allergen Bet v 1 and its homologue in cherry (Prunus avium) Pru av 1 has already been identified. This is the so-called ‘P-loop’ region, which encompasses amino acid residues around position 45 and is found on the two virtually identical tertiary protein structures. We tried to determine an additional IgE cross-reacting patch on Pru av 1 and Bet v 1. The putative IgE-binding region on Pru av 1 was localized with a mAb (monoclonal antibody) that was generated against Bet v 1, and cross-reacts with several Bet v 1 homologues in food and inhibits the binding of patients' IgE to Pru av 1. mAb reactivity pattern was analysed and amino acid positions 28 and 108 of Pru av 1 were selected and mutated by site-directed mutagenesis. The Pru av 1 mutants were produced as recombinant proteins and characterized for their folding, mAb- and IgE-binding capacity and allergenic potency with a cellular assay using the humanized rat basophilic leukaemia cell line RBL-25/30. Amino acid position 28 is involved in a second major IgE-binding region on Pru av 1 and probably on Bet v 1. The identification of this second major IgE-binding region is an essential prerequisite to understand the phenomenon of cross-reactivity and its clinical consequences, and to produce hypoallergenic proteins for an improved immunotherapy of type I allergy.
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Research Article|
December 14 2004
Molecular basis of pollen-related food allergy: identification of a second cross-reactive IgE epitope on Pru av 1, the major cherry (Prunus avium) allergen
Regina WICHE;
Regina WICHE
*Division of Allergology, Paul-Ehrlich-Institut, Paul-Ehrlich-Strasse 51–59, 63225 Langen, Germany
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Michaela GUBESCH;
Michaela GUBESCH
*Division of Allergology, Paul-Ehrlich-Institut, Paul-Ehrlich-Strasse 51–59, 63225 Langen, Germany
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Herbert KÖNIG;
Herbert KÖNIG
†Division of Haematology and Transfusion Medicine, Paul-Ehrlich-Institut, Paul-Ehrlich-Strasse 51–59, 63225 Langen, Germany
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Kay FÖTISCH;
Kay FÖTISCH
*Division of Allergology, Paul-Ehrlich-Institut, Paul-Ehrlich-Strasse 51–59, 63225 Langen, Germany
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Andreas HOFFMANN;
Andreas HOFFMANN
*Division of Allergology, Paul-Ehrlich-Institut, Paul-Ehrlich-Strasse 51–59, 63225 Langen, Germany
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Andrea WANGORSCH;
Andrea WANGORSCH
*Division of Allergology, Paul-Ehrlich-Institut, Paul-Ehrlich-Strasse 51–59, 63225 Langen, Germany
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Stephan SCHEURER;
Stephan SCHEURER
*Division of Allergology, Paul-Ehrlich-Institut, Paul-Ehrlich-Strasse 51–59, 63225 Langen, Germany
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Stefan VIETHS
Stefan VIETHS
1
*Division of Allergology, Paul-Ehrlich-Institut, Paul-Ehrlich-Strasse 51–59, 63225 Langen, Germany
1To whom correspondence should be addressed (email viest@pei.de).
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Publisher: Portland Press Ltd
Received:
May 20 2004
Revision Received:
July 25 2004
Accepted:
August 27 2004
Accepted Manuscript online:
August 27 2004
Online ISSN: 1470-8728
Print ISSN: 0264-6021
The Biochemical Society, London
2005
Biochem J (2005) 385 (1): 319–327.
Article history
Received:
May 20 2004
Revision Received:
July 25 2004
Accepted:
August 27 2004
Accepted Manuscript online:
August 27 2004
Citation
Regina WICHE, Michaela GUBESCH, Herbert KÖNIG, Kay FÖTISCH, Andreas HOFFMANN, Andrea WANGORSCH, Stephan SCHEURER, Stefan VIETHS; Molecular basis of pollen-related food allergy: identification of a second cross-reactive IgE epitope on Pru av 1, the major cherry (Prunus avium) allergen. Biochem J 1 January 2005; 385 (1): 319–327. doi: https://doi.org/10.1042/BJ20040842
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