title: Relevant B cell epitopes in allergic disease.
abstract: The 3-dimensional structure of an allergen defines the accessible parts on the surface of the molecule or epitopes that interact with antibodies. Mapping the antigenic determinants for IgE antibody binding has been pursued through strategies based on the use of overlapping synthetic peptides, recombinant allergenic fragments or unfolded allergens. These approaches led to the identification of mostly linear epitopes and are useful for food allergens that undergo digestion or food processing. For inhaled allergens, conformational epitopes appear to be the primary targets of IgE responses. Knowledge of the molecular structure of allergens alone and in complex with antibodies that interfere with IgE antibody binding is important to understand the immune recognition of B cell-antigenic determinants on allergens and the design of recombinant allergens for immunotherapy. Starting with the molecular cloning and expression of allergens, and with the advent of X-ray crystallography and nuclear magnetic resonance techniques, we have been able to visualize conformational epitopes on allergens.
authors: Indoor Biotechnologies, Inc., Charlottesville, Va., USA. apomes@inbio.com
authors: Anna
authors: A
authors: Pomés
mesh_terms: D000818:Animals; D016282:Aspartic Acid Endopeptidases / Q000737:chemistry / Q000276:immunology / Q000378:metabolism; D018604:Epitope Mapping; D018985:Epitopes, B-Lymphocyte / Q000737:chemistry / Q000276:immunology*; D006801:Humans; D006967:Hypersensitivity / Q000276:immunology*; D007140:Immunoglobulin Fab Fragments / Q000737:chemistry / Q000276:immunology / Q000378:metabolism; D008958:Models, Molecular
chemical_list: D018985:Epitopes, B-Lymphocyte; D007140:Immunoglobulin Fab Fragments; D016282:Aspartic Acid Endopeptidases; C094699:allergen Bla g 2