Structural Basis for the IgE-Binding Cross-Reacting Epitopic Peptides of Cup s 3, a PR-5 Thaumatin-like Protein Allergen from Common Cypress (Cupressus sempervirens) Pollen

The present work was aimed at identifying the IgE-binding epitopic regions on surface of Cup s 3 allergen from common cypress Cupressus sempervirens, that are possibly involved in cross-reactivity reported between Cupressaceae species. Three main were mapped molecular 3, PR-5 thaumatin-like sempervirens. They correspond to exposed areas containing either electropositive (R, K) or electronegative (D, E) residues. A coalescence occurs epitopes #1 and #2, creates an extended allergen. Epitope #3 contains a putative N-glycosylation site which is actually glycosylated could therefore comprise glycotope. However, most allergenic potency depends non-glycosylated peptides. corresponding allergens other closely related (Cryptomeria, Juniperus, Thuja) exhibit very similar conformation should account for observed among allergens.