title: Structural bioinformatic approaches to understand cross-reactivity.
abstract: Cross-reactivity of allergens results from the presence of antibody-accessible conserved surface structures. These can best be studied when allergens have been structurally defined by X-ray crystallography or another structure determination method. When this is not the case, mimotope technology provides a useful alternative for elucidating antibody-binding sites on allergens. Structural bioinformatic approaches have been used to study the cross-reactivity of inhalant allergens with labile food allergens (Bet v 1 family) as well as the cross-reactivity between stable food allergens such as members of the nonspecific lipid transfer protein family. It was found that the degree of similarity of the structures correlated with the observed IgE cross-reactivities. However, IgE cross-reactivity between structurally unrelated allergens has not been demonstrated to date.
authors.affiliation: Department of Pathophysiology, Medical University of Vienna, Vienna, Austria. Heimo.Breiteneder@meduniwien.ac.at
authors.forename: Heimo
authors.initials: H
authors.lastname: Breiteneder
authors.forename: Clare
authors.initials: C
authors.lastname: Mills
mesh_terms: D000485:Allergens / Q000276:immunology*; D000595:Amino Acid Sequence; D000918:Antibody Specificity; D001666:Binding Sites, Antibody; D019295:Computational Biology; D007073:Immunoglobulin E / Q000276:immunology*; D010940:Plant Proteins / Q000737:chemistry / Q000276:immunology; D011506:Proteins / Q000737:chemistry* / Q000276:immunology*; D017385:Sequence Homology
chemical_list: D000485:Allergens; D010940:Plant Proteins; D011506:Proteins; D007073:Immunoglobulin E