The Journal of Allergy and Clinical Immunology
Volume 124, Issue 6 , Pages 1273-1281.e2, December 2009

Assessment of component-resolved in vitro diagnosis of celeriac allergy

  • Kerstin Bauermeister, MSc

      Affiliations

    • Paul-Ehrlich-Institut, Langen, Germany
  • ,
  • Barbara K. Ballmer-Weber, MD

      Affiliations

    • Department of Dermatology, University Hospital Zurich, Zurich, Switzerland
  • ,
  • Merima Bublin, PhD

      Affiliations

    • Department of Pathophysiology, Medical University of Vienna, Vienna, Austria
  • ,
  • Philipp Fritsche, MD

      Affiliations

    • Department of Dermatology, University Hospital Zurich, Zurich, Switzerland
  • ,
  • Kay-Martin O. Hanschmann, MSc

      Affiliations

    • Paul-Ehrlich-Institut, Langen, Germany
  • ,
  • Karin Hoffmann-Sommergruber, PhD

      Affiliations

    • Department of Pathophysiology, Medical University of Vienna, Vienna, Austria
  • ,
  • Jonas Lidholm, PhD

      Affiliations

    • Phadia AB, Uppsala, Sweden
  • ,
  • Christina Oberhuber, PhD

      Affiliations

    • Biomay AG, Vienna, Austria
  • ,
  • Stefanie Randow

      Affiliations

    • Paul-Ehrlich-Institut, Langen, Germany
  • ,
  • Thomas Holzhauser, PhD

      Affiliations

    • Paul-Ehrlich-Institut, Langen, Germany
  • ,
  • Stefan Vieths, PhD

      Affiliations

    • Paul-Ehrlich-Institut, Langen, Germany
    • Corresponding Author InformationReprint requests: Stefan Vieths, PhD, Paul-Ehrlich-Institut, Paul-Ehrlich-Str 51-59, 63225 Langen, Germany.

Received 17 March 2009; received in revised form 8 June 2009; accepted 14 July 2009. published online 05 October 2009.

Background

Previous studies have demonstrated insufficient sensitivity of commercially available celeriac extract reagents in the diagnosis of celeriac allergy.

Objective

We sought to assess the diagnostic performance of specific IgE determination based on recombinant and purified natural celeriac allergens in comparison with an extract-based assay and to investigate interference by IgE to cross-reactive carbohydrate determinants and its biologic activity.

Methods

Twenty-four subjects with a positive double-blind, placebo-controlled food challenge result to celeriac; 20 atopic control subjects with birch pollen allergy who tolerated celeriac; and 20 nonatopic subjects were enrolled. IgE binding was investigated for celeriac allergens (rApi g 1.01, rApi g 4, and nApi g 5), extract reagents (celeriac, birch, mugwort, and timothy grass pollen), birch pollen allergens (rBet v 1 and rBet v 2), and cross-reactive carbohydrate determinants by means of ImmunoCAP analysis. Biologic activity of allergens was determined based on basophil mediator release.

Results

Component-resolved ImmunoCAP analysis considerably increased the sensitivity to detect celeriac-specific IgE by 20%. Sensitization to carbohydrate structures was detected in 38% of patients with celeriac allergy, and there was an excellent correlation between sensitization to the glycoprotein Api g 5 and isolated glycan. Positive results among atopic control subjects were mainly caused by protein allergens, whereas the effect of carbohydrate epitopes was marginal. The ability of allergens to induce mediator release decreased in the order Bet v 1 > Api g 1 > Api g 5, confirming the low biologic activity of IgE to carbohydrate epitopes.

Conclusion

Component-resolved diagnosis allowed an increase in diagnostic sensitivity from 67% to 88% compared with extract-based diagnosis. Sensitization to Api g 5 was attributable to its glycan moieties but did not interfere with diagnostic specificity.

Key words: Component-resolved diagnosis, celeriac allergy, ImmunoCAP, recombinant allergens, cross-reactive carbohydrate determinants, pollen-related food allergy, cross-reactivity

Abbreviations used: CCD, Cross-reactive carbohydrate determinant, CRD, Component-resolved diagnosis, DBPCFC, Double-blind, placebo-controlled food challenge, MUXF3, Glycan structure Manα1-6(Xylβ1-2)Manβ1-4GlcNAcβ1-4(Fucα1-3)GlcNAc, OAS, Oral allergy syndrome, PR-10, Pathogenesis-related class 10 protein, RBL, Rat basophilic leukemia

 

 K. B. was supported by the European Commission, EuroPrevall “The Prevalence, Cost and Basis of Food Allergy across Europe,” contract no. 514000. M. B. was supported in part by the Austrian Science Fund, grant SFB F01802.

 Disclosure of potential conflict of interest: J. Lidholm is employed by Phadia. T. Holzhauser has served as a scientific expert and speaker for Allergenicity Assessment, Internation Life Science Institute ILSI-HESI; has served as a consultant on analytic methods for IFP Berlin; and has received research support from the European Commission EU-Project EuroPrevall. S. Vieths is an associate for the Institute for Product Quality, Berlin, Germany; has received honoraria from Phadia, the Food Allergy Resource and Research Program (United States), and Mars Chocolate UK Ltd and Mars Nederland BV; has received research support from the European Union (EuroPrevall), the German Research Society, the Research Fund of the German Food Industry, Monsanto Company, Pioneer Hi-Breed International, and the European Directorate for Quality of Medicines and Healthcare; is the Chairman of the Food Allergy Interest Group for the European Academy of Allergy and Clinical Immunology and the Chairman of the Allergen Standardization Subcommittee and the Secretary of the Allergen Nomenclature Subcommittee for the International Union of Immunological Societies, a registered expert with the European Agency for the Evaluation of Medicinal Products and the European Pharmacopeia Commission, is the chairman of Technical Committee 275 of the CEN; and is a member of the Food Allergy Working Group for the German Society for Allergy and Clinical Immunology. The rest of the authors have declared that they have no conflict of interest.

PII: S0091-6749(09)01126-9

doi:10.1016/j.jaci.2009.07.033

The Journal of Allergy and Clinical Immunology
Volume 124, Issue 6 , Pages 1273-1281.e2, December 2009