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Identification of IgE binding to Api g 1-derived peptides.
Chembiochem 2010; 11(16):2283-93C

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.

Authors+Show Affiliations

Allergie-Centrum-Charité, Klinik für Dermatologie und Allergologie, Charité-Universitätsmedizin Berlin, Berlin, Germany.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

20872390

Citation

Ruppel, Elvira, et al. "Identification of IgE Binding to Api G 1-derived Peptides." Chembiochem : a European Journal of Chemical Biology, vol. 11, no. 16, 2010, pp. 2283-93.
Ruppel E, Aÿ B, Boisguerin P, et al. Identification of IgE binding to Api g 1-derived peptides. Chembiochem. 2010;11(16):2283-93.
Ruppel, E., Aÿ, B., Boisguerin, P., Dölle, S., Worm, M., & Volkmer, R. (2010). Identification of IgE binding to Api g 1-derived peptides. Chembiochem : a European Journal of Chemical Biology, 11(16), pp. 2283-93. doi:10.1002/cbic.201000322.
Ruppel E, et al. Identification of IgE Binding to Api G 1-derived Peptides. Chembiochem. 2010 Nov 2;11(16):2283-93. PubMed PMID: 20872390.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Identification of IgE binding to Api g 1-derived peptides. AU - Ruppel,Elvira, AU - Aÿ,Bernhard, AU - Boisguerin,Prisca, AU - Dölle,Sabine, AU - Worm,Margitta, AU - Volkmer,Rudolf, PY - 2010/9/28/entrez PY - 2010/9/28/pubmed PY - 2011/2/12/medline SP - 2283 EP - 93 JF - Chembiochem : a European journal of chemical biology JO - Chembiochem VL - 11 IS - 16 N2 - 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. SN - 1439-7633 UR - https://www.unboundmedicine.com/medline/citation/20872390/Identification_of_IgE_binding_to_Api_g_1_derived_peptides_ L2 - https://doi.org/10.1002/cbic.201000322 DB - PRIME DP - Unbound Medicine ER -