IgE and IgG antibodies of patients with allergy to birch pollen as tools to define the allergen profile of <i>Betula verrucosa</i>*

Jarolim, E.; Rumpold, Helmut; Endler, Anne; Ebner, H; Breitenbach, Michael; Scheiner, Otto; Kraft, Dietrich

doi:10.1111/j.1398-9995.1989.tb04169.x

Cited by 216 publications

(175 citation statements)

References 23 publications

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“…Although the role of allergen-specific IgG responses after allergen exposure (24,25 ) has remained controversial (26,27 ), the production of high-affinity IgG antibodies during SIT is of particular interest because Fig. 3.…”

Section: Discussionmentioning

confidence: 99%

Generation of Human Monoclonal Allergen-Specific IgE and IgG Antibodies from Synthetic Antibody Libraries

et al. 2007

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Background: Allergen-specific IgE and IgG antibodies play pivotal roles in the induction and progression of allergic hypersensitivity reactions. Consequently, monoclonal human IgE and IgG4 antibodies with defined specificity for allergens should be useful in allergy research and diagnostic tests. We used combinatorial antibody libraries and subsequent recombinant production to make and assess IgE, IgG1, and IgG4 allergen-specific antibodies. Methods: We used phage display to select a synthetic single-chain antibody fragment (scFv) library against 3 different allergens, from bee venom, bovine milk, and apple. The scFv obtained were converted into IgG1, IgG4, and IgE antibody formats and assessed for their biochemical properties by ELISA, immunoblotting, and fluorescence-activated cell sorting. Results: Two different antibody formats for each IgG1, IgG4, and IgE antibody were produced in mammalian cells as disulfide-linked and glycosylated Ig, which were usable in allergen-specific ELISA assays and immunoblots. In addition, the recombinant IgE antibodies mediated the binding of allergens to HEK-293 cells transfected with the high-affinity IgE receptor, and this binding was blocked by corresponding IgG antibodies. Conclusions: The use of synthetic libraries for the generation of allergen-specific recombinant IgE and IgG

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Section: Discussionmentioning

confidence: 99%

Generation of Human Monoclonal Allergen-Specific IgE and IgG Antibodies from Synthetic Antibody Libraries

et al. 2007

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“…More than 95% of birch pollen-allergic patients are sensitized against the major birch pollen allergen, Bet v 1 (17,18). Recently we produced by genetic engineering two recombinant fragments of Bet v 1 comprising aa 1-74 and aa 75-160 (26).…”

Section: Discussionmentioning

confidence: 99%

“…Here we report the characterization of recombinant hypoallergenic fragments of the major birch pollen allergen, Bet v 1, as candidate molecules for specific immunotherapy. Bet v 1 is recognized by Ͼ95% of birch pollen allergic patients, and 60% of these patients react exclusively with this allergen (17,18). The cDNA coding for Bet v 1 was isolated (19), and recombinant Bet v 1, which has immunological and biological properties comparable to natural Bet v 1 (18,20) and shares epitopes with homologous proteins present in the pollen of trees of the order Fagales and in plant-derived food was produced in Escherichia coli (21)(22)(23)(24).…”

mentioning

confidence: 99%

T Cell Epitope-Containing Hypoallergenic Recombinant Fragments of the Major Birch Pollen Allergen, Bet v 1, Induce Blocking Antibodies

Vrtala

Akdiş²,

Budak³

et al. 2000

The Journal of Immunology

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Allergen-specific immunotherapy represents one of the few curative approaches toward type I allergy. Up to 25% of allergic patients are sensitized against the major birch pollen allergen, Bet v 1. By genetic engineering we produced two recombinant (r) Bet v 1 fragments comprising aa 1–74 and aa 75–160 of Bet v 1, which, due to a loss of their native-like fold, failed to bind IgE Abs and had reduced allergenic activity. Here we show that both fragments covering the full Bet v 1 sequence induced human lymphoproliferative responses similar to rBet v 1 wild type. The C-terminal rBet v 1 fragment induced higher lymphoproliferative responses than the N-terminal fragment and represented a Th1-stimulating segment with high IFN-γ production, whereas the N-terminal fragment induced higher IL-4, IL-5, and IL-13 secretion. Immunization of mice and rabbits with rBet v 1 fragments induced IgG Abs, which cross-reacted with complete Bet v 1 and Bet v 1-related plant allergens and strongly inhibited the IgE binding of allergic patients to these allergens. Thus, our results demonstrate that hypoallergenic T cell epitope-containing rBet v 1 fragments, despite lacking IgE epitopes, can induce Abs in vivo that prevent the IgE binding of allergic patients to the wild-type allergen. The overall demonstration of the immunogenic features of the hypoallergenic rBet v 1 fragments will now enable clinical studies for safer and more efficient specific immunotherapy.

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“…Aqueous extracts of these pollens were prepared as previously described [2] and resolved in double-distilled water. Biocryl BPA 1000 (TosoHaas) was added (2500 parts/ million) followed by centrifugation in an Eppendorf centrifuge for 10min.…”

Section: Allergen Protein Preparationsmentioning

confidence: 99%

“…IgE immunoblots were performed according to procedures described previously [2]. Protein estimation was performed before loading identical protein amounts onto SDSI polyacrylamide gels in order to make comparison of the IgEbinding capacities of Cor a 1 isoforms possible [8].…”

Section: Ige Immunoblotsmentioning

confidence: 99%

Four Recombinant Isoforms of Cor a 1, the Major Allergen of Hazel Pollen, Show Different Reactivities with Allergen‐specific T‐lymphocyte Clones

Schenk

Hoffmann‐Sommergruber

Breiteneder

et al. 1994

European Journal of Biochemistry

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Purified preparations of allergenic proteins from plants, and in particular from pollens, consist of multiple closely related isoforms. These isoforms are highly similar in their amino acid sequences, yet they display different properties with respect to antibody binding. In this study we report of differential potencies of cross-reacting tree pollen allergens and cloned isoforms of these allergens to activate allergen-specific T-lymphocyte clones (T-cell clones ; TCC). Six TCC with specifity for Bet v 1, a representative tree pollen major allergen, were established from peripheral blood of five birch-pollen-allergic donors. All TCC displayed the helper-cell phenotype. Five TCC reacted with distinct epitopes present on natural (n) and on recombinant (r) Bet v 1. One TCC could not be stimulated with r Bet v 1, in spite of strong reactivity with purified natural Bet v 1. The TCC were tested in proliferation assays using purified n Bet v 1, n Cor a 1 (the homologous major allergen of hazel pollen), r Bet v 1, four recombinant isoforms of Cor a 1 and peptides representing corresponding T-cell stimulating regions (isoepitopes) on these proteins. The clones showed different patterns of reactivity in response to stimulation with the five recombinant molecules and the corresponding peptides. Certain exchanges of amino acids within stimulating peptides correlated with a lack of proliferation of the TCC tested. These findings are important with respect to the use of broadly cross-reactive recombinant allergens or allergen-derived peptides for immunotherapy of type I allergy.Type I allergy to tree pollens is very common in the northern hemisphere. In this respect, pollens from trees of the order Fagales, in particular birch, hazel and alder, represent the most important sources of allergens [l, 21. The major allergens of these pollens (Bet v 1, Cor a 1 and A h g 1) show a high degree of similiarity at the nucleic acid 131 and at the amino acid levels [4], and cross-reactivity was described for IgE antibodies [5] and for T-cell clones (TCC) [6]. This fits well with the observation that tree pollen-allergic patients develop symptoms when exposed to pollens from all these tree species.Natural allergens consist of multiple isoallergens [7 -91. Recently, four isoforms of Cor a 1, the major allergen of hazel pollen, were cloned, sequenced and expressed as recombinant non-fusion proteins [8]. Comparison of the amino acid sequences of these Cor a 1 isoforms revealed identities Correspondence to

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IgE and IgG antibodies of patients with allergy to birch pollen as tools to define the allergen profile of *Betula verrucosa**

Cited by 216 publications

References 23 publications

Generation of Human Monoclonal Allergen-Specific IgE and IgG Antibodies from Synthetic Antibody Libraries

Generation of Human Monoclonal Allergen-Specific IgE and IgG Antibodies from Synthetic Antibody Libraries

T Cell Epitope-Containing Hypoallergenic Recombinant Fragments of the Major Birch Pollen Allergen, Bet v 1, Induce Blocking Antibodies

Four Recombinant Isoforms of Cor a 1, the Major Allergen of Hazel Pollen, Show Different Reactivities with Allergen‐specific T‐lymphocyte Clones

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IgE and IgG antibodies of patients with allergy to birch pollen as tools to define the allergen profile of Betula verrucosa*

Cited by 216 publications

References 23 publications

Generation of Human Monoclonal Allergen-Specific IgE and IgG Antibodies from Synthetic Antibody Libraries

Generation of Human Monoclonal Allergen-Specific IgE and IgG Antibodies from Synthetic Antibody Libraries

T Cell Epitope-Containing Hypoallergenic Recombinant Fragments of the Major Birch Pollen Allergen, Bet v 1, Induce Blocking Antibodies

Four Recombinant Isoforms of Cor a 1, the Major Allergen of Hazel Pollen, Show Different Reactivities with Allergen‐specific T‐lymphocyte Clones

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IgE and IgG antibodies of patients with allergy to birch pollen as tools to define the allergen profile of *Betula verrucosa**