IgE cross‐reactivity between birch pollen, mugwort pollen and celery is due to at least three distinct cross‐reacting allergens: immunoblot investigation of the birch‐mugwort‐celery syndrome

Bauer, Leonhardt; Ebner, Christof; Hirschwehr, Reinhold; Wüthrich, B; Pichler, C. E.; Fritsch, R; Scheiner, Otto; Kraft, Dietrich

doi:10.1111/j.1365-2222.1996.tb00503.x

Cited by 123 publications

(116 citation statements)

References 32 publications

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“…34 In many cases overall sensitization to immunodominant proteins, as well as individual sensitization to minor allergenic proteins, was observed. [ [40] Immunodominant proteins with identical or highly similar molecular masses were detected in extracts of different sources, indicating food-pollen 41 or food-food crossreactivity. [35], [36], [42] and [43] Preabsorption of patient serum with purified native or recombinant allergenic molecules before immunoblot experiments confirmed the expression of cross-reactive sIgEs, which are capable of binding proteins from different sources with conserved binding sides and sufficient sequential, as well as structural, homology.…”

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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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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“…4 the immunodominant region is highlighted within a computer model of the Art v 1 molecule. Further T cell-stimulating peptides could be identified in the sequence area Art v 1 [1][2][3][4][5][6][7][8][9][10][11][12][13][14][15][16][17][18] and Art v 1 40 -55 . The nArt v 1-specific TCC that did not cross-react with rArt v 1 could not be stimulated with any of the peptides synthesized according to rArt v 1.…”

Section: T Cell Epitopes and Tcr V␤ Usagementioning

confidence: 99%

“…Being the major allergen in mugwort pollen, it was termed Art v 1. 3 It does not belong to the proteins that cross-react in the so-called birchmugwort-celery syndrome (8), but it cross-reacts with a homologous protein in ragweed (7) that is not yet defined on a molecular basis. The cDNA sequence of Art v 1 was determined, and the correlating protein was expressed as recombinant nonfusion protein in Escherichia coli and purified to homogeneity.…”

Section: T He Family Of Compositae Ormentioning

confidence: 99%

The T Cell Response to Art v 1, the Major Mugwort Pollen Allergen, Is Dominated by One Epitope

Jahn‐Schmid

Kelemen

Himly

et al. 2002

The Journal of Immunology

104

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Mugwort (Artemisia vulgaris) pollen allergens represent the main cause of pollinosis in late summer in Europe. At least 95% of sera from mugwort pollen-allergic patients contain IgE against a highly glycosylated 24- to 28-kDa glycoprotein. Recently, this major allergen, termed Art v 1, was characterized, cloned in Escherichia coli, and produced in recombinant form. In the present study we characterized and compared the T cell responses to natural (nArt v 1) and recombinant Art v 1 (rArt v 1). In vitro T cell responses to nArt v 1 and rArt v 1 were studied in PBMC, T cell lines (TCL), and T cell clones (TCC) established from PBMC of mugwort-allergic patients. Stimulation of PBMC or allergen-specific TCL with either nArt v 1 or rArt v 1 resulted in comparable proliferative T cell responses. Eighty-five percent of the TCC reactive with rArt v 1 cross-reacted with the natural protein. The majority of the CD4+CD8−TCR αβ+ Art v 1-specific TCC, obtained from 10 different donors, belonged to the Th2 phenotype. Epitope mapping of TCL and TCC using overlapping peptides revealed a single immunodominant T cell epitope recognized by 81% of the patients. Inhibition experiments demonstrated that the presentation of this peptide is restricted by HLA-DR molecules. In conclusion, the T cell response to Art v 1 is characterized by one strong immunodominant epitope and evidently differs from the T cell responses to other common pollen allergens known to contain multiple T cell epitopes. Therefore, mugwort allergy may be an ideal candidate for a peptide-based immunotherapy approach.

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“…Recently, a third group of proteins, other than Bet V 1, Bet v 2, and their homologs, displaying IgE cross-reactivity shared by birch, mugwort pollen, and celery, has been identified (20). Tliese proteins have a molecular range of 46-60 kDa.…”

Section: Results and Discnssionmentioning

confidence: 99%

Pollen cross‐reactivity. Can we establish a link between the in vitro results and the clinical situation?

Wüthrich

Straumann

1997

Allergy

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IgE cross‐reactivity between birch pollen, mugwort pollen and celery is due to at least three distinct cross‐reacting allergens: immunoblot investigation of the birch‐mugwort‐celery syndrome

Abstract: Therefore we propose, from a serological point of view, to extend the mugwort-celery syndrome to the birch-mugwort-celery syndrome.

Cited by 123 publications

References 32 publications

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

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

The T Cell Response to Art v 1, the Major Mugwort Pollen Allergen, Is Dominated by One Epitope

Pollen cross‐reactivity. Can we establish a link between the in vitro results and the clinical situation?

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