Identification of IgE Binding to Api g 1‐Derived Peptides
- 24 September 2010
- journal article
- research article
- Published by Wiley in ChemBioChem
- Vol. 11 (16), 2283-2293
- https://doi.org/10.1002/cbic.201000322
Abstract
Celery is a frequent cause of food allergy in pollen-sensitized patients and can induce severe allergic reactions. Clinical symptoms cannot be predicted by skin prick tests (SPTs) or by determining allergen-specific immunoglobulin E (IgE). Our aim was to identify specific IgE binding peptides by using an array technique. For our study, the sera of 21 patients with positive double-blind, placebo-controlled food challenge (DBPCFC) to celery, as well as the sera of 17 healthy patients were used. Additionally, all patients underwent skin tests along with determinations of specific IgE binding. The major allergen of celery Api g 1.0101 (Apium graveolens) was synthesized as an array of overlapping peptides and probed with the patients' sera. We developed an improved immunoassay protocol by investigating peptide lengths, peptide densities, incubation parameters, and readout systems, which could influence IgE binding. Sera of celery-allergic patients showed binding to three distinct regions of Api g 1.0101. The region including amino acids 100 to 126 of Api g 1.0101 is the most important region for IgE binding. This region caused a fivefold higher binding of IgE from the sera of celery-allergic patients compared to those of healthy individuals. In particular, one peptide (VLVPTADGGSIC) was recognized by all sera of celery-allergic patients. In contrast, no binding to this peptide was detected in sera of the healthy controls. Our improved assay strategy allows us to distinguish between celery-allergic and healthy individuals, but needs to be explored in a larger cohort of well-defined patients.Keywords
This publication has 65 references indexed in Scilit:
- Food allergyJournal of Allergy and Clinical Immunology, 2010
- Bayesian Modeling of the Yeast SH3 Domain Interactome Predicts Spatiotemporal Dynamics of Endocytosis ProteinsPLoS Biology, 2009
- Evidence for Novel Tomato Seed Allergens: IgE-Reactive Legumin and Vicilin Proteins Identified by Multidimensional Protein Fractionation−Mass Spectrometry and in Silico Epitope ModelingJournal of Proteome Research, 2009
- What are the best outcome measurements for atopic eczema? A systematic reviewJournal of Allergy and Clinical Immunology, 2007
- Specificity of IgE antibodies to sequential epitopes of hen's egg ovomucoid as a marker for persistence of egg allergyAllergy, 2007
- Pitfalls in double‐blind, placebo‐controlled oral food challengesAllergy, 2007
- Standard skin prick testing and sensitization to inhalant allergens across Europe – a survey from the GA2LEN network*Allergy, 2005
- Bet v 1142-156 is the dominant T-cell epitope of the major birch pollen allergen and important for cross-reactivity with Bet v 1–related food allergensJournal of Allergy and Clinical Immunology, 2005
- Protein Interaction Networks by Proteome Peptide ScanningPLoS Biology, 2004
- Utility of food-specific IgE concentrations in predicting symptomatic food allergyJournal of Allergy and Clinical Immunology, 2001