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Post-translational modifications influence IgE reactivity to the major allergen Phl p 1 of timothy grass pollen

Post-translational modifications influence IgE reactivity to the major allergen Phl p 1 of timothy grass pollen

Clinical & Experimental Allergy 28(3): 315-321

Background. Grass group I consists of very potent allergenic components which are found in the pollen of all temperate grasses. Several post-translational modifications are predicted from the cDNA data. Objective. The aim of this study was to identify sequential IgE-binding sites on the allergen Ph1 p 1 and to determine their influence on IgE reactivity. Methods. Based on cDNA data and microsequencing results we synthesized overlapping decapeptides covering the complete Ph1 p 1 molecule and tested them for immunological reactivity by means of the PEPSCAN technique. In a dot test we determined the frequency of IgE reactivities to post-translationally modified structures (hydroxylated proline residues, carbohydrate structure, and disulphide formations). Results. Screening by overlapping peptides demonstrated an IgE binding site on the 10 N-terminal amino acids. Comprehensive studies showed that the two hydroxyproline residues of the native Ph1 p 1 allergen (at positions 5 and 8) and the N-glycan (at position 9) can result in an increased IgE reactivity; 3.3% of the sera exclusively bound to the hydroxyproline bearing peptide, while only 0.4% bound to the proline containing peptide. With regard to glycosylation, we estimated that 20% of sera recognized protein and carbohydrate epitopes, while one serum exclusively bound to the glycan. The formation of disulphide bonds has no detectable effect on the IgE reactivity to Ph1 p 1. Conclusion. Our results indicate that the post-translational modifications, the carbohydrate structure and the hydroxylation of proline residues, can enhance the IgE reactivity of Ph1 p 1.

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Accession: 009218318

Download citation: RISBibTeXText

PMID: 9543081

DOI: 10.1046/j.1365-2222.1998.00221.x

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