High-resolution crystal structure and IgE recognition of the major grass pollen allergen Phl p 3.

摘要: Background Group 2 and 3 grass pollen allergens are major with high allergenic activity exhibit structural similarity the C-terminal portion of group 1 allergens. In this study, we aimed to determine crystal structure timothy allergen, Phl p 3, study its IgE recognition cross-reactivity allergens. Methods The three-dimensional was solved by X-ray crystallography compared structures Cross-reactivity studied using a human monoclonal antibody which inhibits allergic patients' binding inhibition experiments sera. Conformational epitopes were predicted algorithm SPADE, variants containing single point mutations in sites produced analyze binding. Results Phl is globular β-sandwich protein showing 1–C-terminal domain. showed but not SPADE identified two conformational epitope-containing areas, one overlaps epitope defined antibody. The mutation arginine 68 alanine completely abolished blocking This D13 second area also reduced binding. Conclusion Group cross-reactive epitopes. They lack relevant therefore need be included diagnostic tests allergen-specific treatments addition