| Autor: |
Bryan R. E. Smith, Kristina Reid Black, Max Bermingham, Sayeh Agah, Jill Glesner, Serge A. Versteeg, Ronald van Ree, Glorismer Pena-Amelunxen, Lorenz Aglas, Scott A. Smith, Anna Pomés, Martin D. Chapman |
| Jazyk: |
angličtina |
| Rok vydání: |
2023 |
| Předmět: |
|
| Zdroj: |
Frontiers in Allergy, Vol 4 (2023) |
| Druh dokumentu: |
article |
| ISSN: |
2673-6101 |
| DOI: |
10.3389/falgy.2023.1270326 |
| Popis: |
IntroductionAllergic reactions are mediated by human IgE antibodies that bind to and cross-link allergen molecules. The sites on allergens that are recognized by IgE antibodies have been difficult to investigate because of the paucity of IgE antibodies in a human serum. Here, we report the production of unique human IgE monoclonal antibodies to major inhaled allergens and food allergens that can be produced at scale in perpetuity.Materials and methodsThe IgE antibodies were derived from peripheral blood mononuclear cells of symptomatic allergic patients, mostly children aged 3–18 years, using hybridoma fusion technology. Total IgE and allergen-specific IgE was measured by ImmunoCAP. Their specificity was confirmed through ELISA and immunoblotting. Allergenic potency measurements were determined by ImmunoCAP inhibition. Biological activity was determined in vitro by comparing β-hexosaminidase release from a humanized rat basophilic cell line.ResultsHuman IgE monoclonal antibodies (n = 33) were derived from 17 allergic patients with symptoms of allergic rhinitis, asthma, atopic dermatitis, food allergy, eosinophilic esophagitis, or red meat allergy. The antibodies were specific for five inhaled allergens, nine food allergens, and alpha-gal and had high levels of IgE (53,450–1,702,500 kU/L) with ratios of specific IgE to total IgE ranging from |
| Databáze: |
Directory of Open Access Journals |
| Externí odkaz: |
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