IgE reactivity to Api g 1, a major celery allergen, in a Central European population is based on primary sensitization by Bet v 1☆☆☆★

Hoffmann‐Sommergruber, Karin; Demoly, Pascal; Crameri, Reto; Breiteneder, Heimo; Ebner, Christof; Laimer, Margit; Blaser, Kurt; Ismail, Chaim; Scheiner, Otto; Bousquet, Jean; Menz, G

doi:10.1016/s0091-6749(99)70397-0

Cited by 64 publications

(41 citation statements)

References 27 publications

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“…In addition to the major band migrating at 17 kDa, an additional, fainter band around 34 kDa was detected by specific IgE by the more sensitive IgE immunoblot. Bet v 1 and homologous proteins tend to form dimers as has been shown for Bet v 1 and Api g 1 previously [34,35,36]. Six out of 9 sera showed decreased binding to rMal d 1mut when compared to rMal d 1wt.…”

Section: Discussionsupporting

confidence: 66%

“…For some samples, a fainter band at approximately 34 kDa was also evident representing the dimeric forms of rMal d 1wt, rBet v 1wt, and rBet v 1mut as it has previously been shown for rBet v 1 and rApi g 1 (fig. 3a, lanes 2, 5, 9 for rMal d 1wt, lanes 2, 5, 8, 9 for rBet v 1wt and lanes 5, 9 for rBet v 1mut [34,35,36]. IgE reactivity to rMal d 1wt was less strong compared to the IgE reactivity to rBet v 1wt.…”

Section: Resultsmentioning

confidence: 99%

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Mutational Analysis of Amino Acid Positions Crucial for IgE-Binding Epitopes of the Major Apple <i>(Malus domestica)</i> Allergen, Mal d 1

Gadermaier

Bohle

et al. 2005

Int Arch Allergy Immunol

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Background: Individual amino acid residues of the major birch pollen allergen, Bet v 1, have been identified to be crucial for IgE recognition. The objective of the present study was to evaluate whether this concept was applicable for the Bet v 1-homologous apple allergen, Mal d 1. Methods: A Mal d 1 five-point mutant was produced by PCR techniques, cloned into pMW 172 and expressed in Escherichia coli BL21(DE3) cells. To evaluate the allergenic properties of the engineered protein compared to Mal d 1 wild-type IgE immunoblotting, ELISA, peripheral blood monocytes proliferation assays, and skin prick tests were performed. Results: The Mal d 1 mutant showed reduced capacity to bind specific IgE as compared to wild-ype Mal d 1 in in vitro assays in the majority of the sera tested. In ELISA, 10 out of 14 serum samples displayed an 88–30% decrease in IgE binding to Mal d 1 mutant compared to wild-type Mal d 1. Skin prick tests in apple-allergic patients (n = 2) confirmed the markedly decreased ability of the Mal d 1 mutant to induce allergic reactions in vivo. However, the relevant T cell epitopes were present in the mutated molecule according to peripheral blood mononuclear cell proliferation assays. Conclusions: Our findings suggest that it is possible to modulate the IgE-binding properties of allergens by single amino acid substitutions at crucial positions which might be useful for future immunotherapy of birch-pollen-associated food allergies which are not ameliorated by birch pollen immunotherapy.

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Section: Discussionsupporting

confidence: 66%

Section: Resultsmentioning

confidence: 99%

Mutational Analysis of Amino Acid Positions Crucial for IgE-Binding Epitopes of the Major Apple <i>(Malus domestica)</i> Allergen, Mal d 1

Gadermaier

Bohle

et al. 2005

Int Arch Allergy Immunol

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“…Prominent examples of them are profilins (38), lipid transfer proteins (39), and cyclophilins (20). They are responsible for oftenobserved clinical syndromes like birch-mugwort-celery syndrome (40), oral allergy syndromes (41), and AE/dermatitis syndrome (42). Perhaps the most interesting class of pan-allergens includes environmental allergens sharing structural homology to self-Ags.…”

Section: Discussionmentioning

confidence: 99%

Cross-Reactivity and 1.4-Å Crystal Structure ofMalassezia sympodialisThioredoxin (Mala s 13), a Member of a New Pan-Allergen Family

Limacher¹,

Glaser²,

Meier³

et al. 2007

The Journal of Immunology

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We have identified thioredoxins (Trx) of Malassezia sympodialis, a yeast involved in the pathogenesis of atopic eczema, and of Aspergillus fumigatus, a fungus involved in pulmonary complications, as novel IgE-binding proteins. We show that these Trx, including the human enzyme, represent cross-reactive structures recognized by serum IgE from individuals sensitized to M. sympodialis Trx. Moreover, all three proteins were able to elicit immediate-type allergic skin reactions in sensitized individuals, indicating a humoral immune response based on molecular mimicry. To analyze structural elements involved in these reactions, the three-dimensional structure of M. sympodialis Trx (Mala s 13) has been determined at 1.4-Å resolution by x-ray diffraction analysis. The structure was solved by molecular replacement and refined to a crystallographic R factor of 14.0% and a free R factor of 16.8% and shows the typical Trx fold. Mala s 13 shares 45% sequence identity with human Trx and superposition of the solved Mala s 13 structure with those of human Trx reveals a high similarity with a root mean square deviation of 1.11 Å for all Cα atoms. In a detailed analysis of the molecular surface in combination with sequence alignment, we identified conserved solvent-exposed amino acids scattered over the surface in both structures which cluster to patches, thus forming putative conformational B cell epitopes potentially involved in IgE-mediated cross- and autoreactivity.

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“…[6] and [49] It could be demonstrated that Bet v 1-homologous class II food allergens are responsible for immunodominant sIgE reactivity in patients with birch pollen allergy, whereas sera of patients without (birch) pollen allergy frequently react to class I food allergenic lipid transfer proteins of these comestibles. [28], [50], [51] and [52] Taken together, immunoblot experiments are an essential basis for the development of in vivo, as well as in vitro, sIgE test systems with purified allergens. However, an immunoblot detection of sIgEs is not a proof of clinical relevance because a single IgE epitope is sufficient for the in vitro reactivity.…”

Section: Immunoblot Analyses Allow For the Identification Of Target Mmentioning

confidence: 99%

Potential, pitfalls, and prospects of food allergy diagnostics with recombinant allergens or synthetic sequential epitopes

Steckelbroeck¹,

Ballmer‐Weber²,

Vieths³

2008

Journal of Allergy and Clinical Immunology

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This article aims to critically review developments in food allergy diagnostics with regard to the verification of specific IgE antibodies and the identification of the responsible allergens. Results of IgE-binding tests with food extracts are hampered by cross-reactive proteins, low-quality test agents, or both. Specificity can be increased by defining adequate cutoff values, whereas sensitivity can be improved by using high-quality test agents. IgE-binding tests with purified allergens enabled reliable quantification of allergen-specific IgE titers, with higher levels found in individuals with food allergy compared with individuals without food allergy. However, the overlap in individual test reactivity between allergic and nonallergic subjects complicates interpretation. Recombinant allergens and synthetic sequential epitopes enabled detection of sensitization profiles, with IgE specific to several allergens and substructures now being suggested as markers of severity, persistence, or both. However, high-power quantitative studies with larger numbers of patients are required to confirm these markers. This article aims to critically review developments in food allergy diagnostics with regard to the verification of specific IgE antibodies and the identification of the responsible allergens. Results of IgE-binding tests with food extracts are hampered by cross-reactive proteins, low-quality test agents, or both. Specificity can be increased by defining adequate cutoff values, whereas sensitivity can be improved by using high-quality test agents. IgE-binding tests with purified allergens enabled reliable quantification of allergen-specific IgE titers, with higher levels found in individuals with food allergy compared with individuals without food allergy. However, the overlap in individual test reactivity between allergic and nonallergic subjects complicates interpretation. Recombinant allergens and synthetic sequential epitopes enabled detection of sensitization profiles, with IgE specific to several allergens and substructures now being suggested as markers of severity, persistence, or both.However, high-power quantitative studies with larger numbers of patients are required to confirm these markers. IgE-mediated and non-IgE-mediated syndromes, where IgE-mediated manifestations are responsible for the majority of food-induced, immediate-type, immune-mediated hypersensitivity reactions. 3 The development of an IgE-mediated response to food requires a series of molecular and cellular interactions, which involve antigenpresenting cells, T lymphocytes, and B lymphocytes. [4] and [5] Depending on the route of sensitization, food allergy is the result of either genuine reactivity to comestibles through the gastrointestinal tract (class I food allergens) or secondary sensitization to cross-reactive food allergens as a consequence of the initial reactivity to homologous pollen-related allergens (class II food allergens). [6] and [7] The majority of class I food allergens are heat stable and resistan...

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IgE reactivity to Api g 1, a major celery allergen, in a Central European population is based on primary sensitization by Bet v 1☆☆☆★

Cited by 64 publications

References 27 publications

Mutational Analysis of Amino Acid Positions Crucial for IgE-Binding Epitopes of the Major Apple <i>(Malus domestica)</i> Allergen, Mal d 1

Mutational Analysis of Amino Acid Positions Crucial for IgE-Binding Epitopes of the Major Apple <i>(Malus domestica)</i> Allergen, Mal d 1

Cross-Reactivity and 1.4-Å Crystal Structure ofMalassezia sympodialisThioredoxin (Mala s 13), a Member of a New Pan-Allergen Family

Potential, pitfalls, and prospects of food allergy diagnostics with recombinant allergens or synthetic sequential epitopes

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