NDLI: Pollen-related food allergy: cloning and immunological analysis of isoforms and mutants of Mal d 1, the major apple allergen, and Bet v 1, the major birch pollen allergen

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European Journal of Nutrition : Volume 38, Issue 3, July 1999

European Journal of Nutrition : Volume 38, Issue 2, April 1999

European Journal of Nutrition : Volume 38, Issue 1, February 1999

European Journal of Nutrition : Volume 37

European Journal of Nutrition : Volume 36

Pollen-related food allergy: cloning and immunological analysis of isoforms and mutants of Mal d 1, the major apple allergen, and Bet v 1, the major birch pollen allergen

Content Provider	Springer Nature Link
Author	Son, D.Y. Scheurer, S. Hoffmann, A. Haustein, D. Vieths, S.
Copyright Year	1999
Abstract	Background: Mal d 1, the major apple allergen, cross-reacts with IgE specific for the major birch pollen allergen, Bet v 1, and is responsible for birch pollen related food allergy to apple. Isoforms of Bet v 1 showing minor sequence variations display different binding capacitiy for specific IgE antibodies from allergic patients. Moreover, strain-dependent variation of allergenicity has been reported for apples. Objective: To investigate the occurence of strain-dependent isoforms of Mal d 1 which may differ in their allergenic potential, to obtain data on structures essential for binding of Mal d 1 to the antibody, and to gain insights into the structures responsible for its IgE cross-reactivity to Bet v 1. Methods: The cDNA of Mal d 1 from various apple strains was amplified by a PCR strategy based on conserved regions of known Mal d 1-sequences, and sequenced. Two major isoforms of Mal d 1were expressed as recombinant proteins and purified, as were different variants of the major birch pollen allergen, Bet v 1. Together with already existing recombinant birch pollen and apple allergens, these were subjected to allergenicity testing by IgE-immunoblotting, enzyme allergo sorbent test and dose related mediator release. “Hot-spots” for IgE-reactivity were identified by site-directed mutagenesis. Results: Twelve Mal d 1-clones were sequenced from 7 apple varieties and compared to 3 known Mal d 1 sequences. The clones were clustered into two groups, each showing a high degree of sequence identity to one of the known sequences and specific differences to the third sequence. No strain-specific sequences were identified. In contrast, apple strains with reported differences in allergenicity showed different expression levels of the major allergen. Immunologic testing of recombinant allergens revealed high IgE binding capacity of 2 major isoforms, named GD26 and GS29, with a slightly higher IgE binding capacity of DG26. Moreover, the allergenicity was similar to another rMal d 1 reported in the literature, representing the isoform divergent from our clones. Mutational analysis of our Mal d 1 allergens identified serine in position 111 as essential for IgE binding. Allergenicity was almost depleted by changing this residue into a proline. Moreover, the corresponding serine residue, present in position 112 of Bet v 1, was in a similar manner crucial for the allergenicity of the birch pollen allergen. Conclusion: We conclude that divergent allergenicity of apple strains mainly depends on differnet expression levels of the major allergen. Introduction of a proline residue in position 111 of Mal d 1 and in position 112 of Bet v 1 led to a drastic reduction of allergenicity of both the pollen and the food allergen, obviously also removing the cross-reactive epitope. Mutants with reduced IgE-reactivity but maintained T-cell reactivity may represent new candidates for a safer specific immunotherapy with reduced side-effects.
Starting Page	201
Ending Page	215
Page Count	15
File Format	PDF
ISSN	14366207
Journal	European Journal of Nutrition
Volume Number	38
Issue Number	4
e-ISSN	14366215
Language	English
Publisher	Steinkopff-Verlag
Publisher Date	1999-09-01
Publisher Place	Darmstadt
Access Restriction	One Nation One Subscription (ONOS)
Content Type	Text
Resource Type	Article
Subject	Nutrition and Dietetics Medicine

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Recombinant Mal d 1 facilitates sublingual challenge tests of birch pollen‐allergic patients with apple allergy

the major birch pollen allergen Bet v 1

Sublingual immunotherapy with recombinant Mal d 1 downregulates the allergen‐specific Th2 response

Birch pollen immunotherapy inhibits anaphylaxis to the cross-reactive apple allergen Mal d 1 in mice.

Seven different genes encode a diverse mixture of isoforms of Bet v 1, the major birch pollen allergen

Isoforms of Bet v 1, the Major Birch Pollen Allergen, Analyzed by Liquid Chromatography, Mass Spectrometry, and cDNA Cloning

The major birch pollen allergen, Bet v 1, shows ribonuclease activity

Apple Allergy: The cDNA Sequence of the Major Allergen of Apple, Determined by Performing PCR with a Primer Based on the N-Terminal Amino Acid Sequence, is Highly Homologous to the Sequence of the Major Birch Pollen Allergen

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

Pollen-related food allergy: cloning and immunological analysis of isoforms and mutants of Mal d 1, the major apple allergen, and Bet v 1, the major birch pollen allergen

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Seven different genes encode a diverse mixture of isoforms of Bet v 1, the major birch pollen allergen

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Pollen-related food allergy: cloning and immunological analysis of isoforms and mutants of Mal d 1, the major apple allergen, and Bet v 1, the major birch pollen allergen