
Mutational analysis of major IgE‐binding epitopes of recombinant bovine αS1‐casein
Author(s) -
Gaudin JeanCharles,
Rabesona Hanitra,
Nioi Claudia,
Choiset Yvan,
Chobert JeanMarc,
Drouet Martine,
DeneryPapini Sandra,
Haertle Thomas
Publication year - 2011
Publication title -
clinical and translational allergy
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.979
H-Index - 37
ISSN - 2045-7022
DOI - 10.1186/2045-7022-1-s1-p3
Subject(s) - epitope , allergen , recombinant dna , immunoglobulin e , milk allergy , allergy , casein , medicine , epitope mapping , immunology , antibody , computational biology , biochemistry , biology , gene
Background Cow’s milk allergy (CMA) is one of the most widespread human allergies, especially in very young children. One of the main bovine milk allergen is aS1-casein which is considered as intrinsically unfolded protein. Its epitope determinants have been partially characterized using synthetic peptides and crucial amino acid residues for IgE-binding have been identified. However, this very useful approach for epitope characterization neglects local interactions or local structures formed in the fulllength protein and their impact on the accessibility of epitopes for IgE.