IgE and T‐cell responses to high‐molecular weight allergens from bee venom
Kettner, Hughes, Corradin… - Clinical & Experimental …, 1999 - Wiley Online Library
Kettner, Hughes, Corradin, Spertini
Clinical & Experimental Allergy, 1999•Wiley Online LibraryBackground Bee venom contains multiple allergens with a wide distribution of molecular
weight. In contrast with conventional bee venom desensitization, peptide or recombinant
allergen immunotherapy may have to take into account patients' individual patterns of
humoral or cellular response. Objective To study immunoglobulin (Ig) E and T‐cell
responses to high‐molecular weight bee venom allergens≥ 50 kDa. Methods Bee venom
proteins were separated by size exclusion chromatography and fractions were characterized …
weight. In contrast with conventional bee venom desensitization, peptide or recombinant
allergen immunotherapy may have to take into account patients' individual patterns of
humoral or cellular response. Objective To study immunoglobulin (Ig) E and T‐cell
responses to high‐molecular weight bee venom allergens≥ 50 kDa. Methods Bee venom
proteins were separated by size exclusion chromatography and fractions were characterized …
Background
Bee venom contains multiple allergens with a wide distribution of molecular weight. In contrast with conventional bee venom desensitization, peptide or recombinant allergen immunotherapy may have to take into account patients' individual patterns of humoral or cellular response.
Objective
To study immunoglobulin (Ig)E and T‐cell responses to high‐molecular weight bee venom allergens ≥ 50 kDa.
Methods
Bee venom proteins were separated by size exclusion chromatography and fractions were characterized by one and two‐dimensional gel electrophoresis. IgE antibody binding to bee venom fractions was analysed by immunoblotting and T‐cell responses by proliferation assay.
Results
Among 38 bee venom‐hypersensitive patients, IgE recognition pattern of bee venom allergens varied greatly. IgE bound mainly to phospholipase A2 and furthermore to several proteins ≥ 50 kDa (50, 54, 69, 84 and 94 kDa). N‐terminal sequences of these proteins showed no homology with known proteins. In addition, peripheral mononuclear cells from patients as well as from nonatopic donors strongly proliferated in response to those proteins.
Conclusions
Although present in low amounts, high‐molecular weight allergens from bee venom elicit strong IgE and T‐cell responses, and may need to be considered as clinically relevant. Therefore, the development of peptide or recombinant protein‐based immunotherapy for bee venom allergy may require careful characterization of such allergens.
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