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

ABSTRACT:

Background

Group 2 and 3 grass pollen allergens are major allergens with high allergenic activity and exhibit structural similarity with the C-terminal portion of major group 1 allergens. In this study, we aimed to determine the crystal structure of timothy grass pollen allergen, Phl p 3, and to study its IgE recognition and cross-reactivity with group 2 and group 1 allergens.

Methods

The three-dimensional structure of Phl p 3 was solved by X-ray crystallography and compared with the structures of group 1 and 2 grass pollen allergens. Cross-reactivity was studied using a human monoclonal antibody which inhibits allergic patients' IgE binding and by IgE inhibition experiments with patients' sera. Conformational Phl p 3 IgE epitopes were predicted with the algorithm SPADE, and

SUBMITTER: Devanaboyina SC 

PROVIDER: S-EPMC5321515 | biostudies-literature | 2014 Dec

REPOSITORIES: biostudies-literature