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Humanized Mediator Release Assay as a Read-Out for Allergen Potency
Published on: June 29, 2021
Jun o 1, a Cross-reactive Juniperus oxycedrus Allergen With Unique Structural and Immunogenic Properties
Sandra Sivill1, Marcos Viñuela1, Irene Real-Arévalo1,2
1Inmunotek, S.L., Alcalá de Henares, Madrid, Spain.
Summary
Juniperus oxycedrus pollen allergen Jun o 1 is a significant cause of cypress allergy. Its unique protein and carbohydrate structures contribute to IgE binding and cross-reactivity with related allergens.
Area of Science:
- Allergen characterization
- Immunology
- Plant biochemistry
Background:
- Juniperus oxycedrus (Cupressaceae family) is common in the Mediterranean.
- The allergenic potential of J. oxycedrus pollen remains largely uninvestigated.
Purpose of the Study:
- To characterize Jun o 1, a J. oxycedrus allergen.
- To compare Jun o 1 with Cup a 1, a known cypress allergen.
Main Methods:
- Purification of native and recombinant Jun o 1 (rJun o 1) and Cup a 1.
- Characterization using SDS-PAGE, 2D-electrophoresis, Western blot, and mass spectrometry.
- Evaluation of IgE binding, cross-reactivity, and mast cell activation using patient sera and mouse models.
Main Results:
- Jun o 1 exists as multiple isoforms and forms oligomers, unlike Cup a 1.
- IgE binding to Jun o 1 is influenced by both protein and carbohydrate components.
- Jun o 1 showed greater IgE-binding inhibition compared to Cup a 1 in allergic patients from J. oxycedrus regions.
Conclusions:
- Jun o 1 is a relevant major allergen in cypress allergy.
- Structural similarities with Cup a 1 cause cross-reactivity.
- Unique protein-glycan determinants contribute to Jun o 1's specific allergenic properties.
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