Abstract
The structure determination of major allergens is a prerequisite for analyzing surface exposed areas of the allergen and for mapping conformational epitopes. These may be determined by experimental methods including crystallographic and NMR-based approaches or predicted by computational methods. In this review we summarize the existing structural information on allergens and their classification in protein fold families. The currently available allergen-antibody complexes are described and the experimentally obtained epitopes compared. Furthermore we discuss established methods for linear and conformational epitope mapping, putting special emphasis on a recently developed approach, which uses the structural similarity of proteins in combination with the experimental cross-reactivity data for epitope prediction.
Highlights
The three-dimensional structure of clinically relevant allergens is of central importance: (i) It allows the visualization and analysis of surface exposed residues and in combination with experimental or computational methods the actual or putative B-cell epitopes can be elucidated. (ii) Structure can yield information about bound ligands, which may modulate the protein’s allergenicity. (iii) The allergen structure forms the basis for the rational design of hypoallergenic derivatives, which may be generated through various methods
This part is complemented with an analysis and discussion of the actual knowledge on conformational epitopes gained from the structure of allergen-Fab complexes
The IgE-binding allergens BLG and Phl p 2 have the major parts of their epitopes located on b-sheets, (Fig. 4, 4C+6C) whereas Hen egg-white lysozyme (HEL) is the only case with a significant contribution of a-helical amino acid residues
Summary
The three-dimensional structure of clinically relevant allergens is of central importance: (i) It allows the visualization and analysis of surface exposed residues and in combination with experimental or computational methods the actual or putative B-cell epitopes can be elucidated. (ii) Structure can yield information about bound ligands (proteins and/or small molecules), which may modulate the protein’s allergenicity. (iii) The allergen structure forms the basis for the rational design of hypoallergenic derivatives, which may be generated through various methods (point mutations, truncations, mosaic proteins, fusion with carrier proteins, etc.). (ii) Structure can yield information about bound ligands (proteins and/or small molecules), which may modulate the protein’s allergenicity. Most allergens are relatively small, stable and well-structured proteins. They are perfectly suited for structural studies by both X-ray crystallography and NMR spectroscopy. In particular caseins, which based on NMR and circular dichroism (CD) evidence, are intrinsically unstructured. These unstructured allergens might get structured upon interactions with other proteins and/or ligands. In addition we summarize the techniques used for experimental and computational characterization of conformational epitopes This part is complemented with an analysis and discussion of the actual knowledge on conformational epitopes gained from the structure of allergen-Fab complexes
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