Two hypo-allergenic derivatives lacking the dominant linear epitope of Scy p 1 and Scy p 3

Abstract

Scylla paramamosain frequently elicits IgE-mediated type-I hypersensitivity reactions. Molecular candidates for crab allergen-specific immunotherapy have not been studied previously. In this study, reduced and alkylated (red/alk) derivatives with destroyed conformational epitopes and mutant derivatives (mtALLERGEN) with deleted heat/digestion-stable linear epitopes were produced of tropomyosin and myosin light chain. Structural changes and the allergenicity of derivatives was analyzed. Compared with wild-type allergens, red/alk derivatives had dramatically altered protein structures, whereas mtALLERGEN showed slightly structural effects. Enzyme linked immunosorbent assay revealed the heterogeneous epitope-recognition patterns with derivatives among 29 crab-sensitised patients, of whom 13% and 62% recognised conformational and linear epitopes, respectively, whereas 25% recognised both epitope types to the same extent. Furthermore, mtALLERGEN could not bind to IgE or induce basophil activation in some patients. These results imply that hypo-allergenic derivatives of crab myofibril allergens that specifically lacked linear epitopes may serve as viable candidates for immunotherapy.