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Mutational analysis of major IgE-binding epitopes of recombinant bovine αS1-casein
© Gaudin et al; licensee BioMed Central Ltd. 2011
Published: 12 August 2011
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 αS1-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 full-length protein and their impact on the accessibility of epitopes for IgE.
The importance of amino acids previously identified as crucial for IgE-binding was evaluated in the context of the whole protein. The binding of αS1-casein specific IgE from 14 patients with CMA on recombinant αS1-casein and two mutant forms in which critical amino acid residues for IgE-binding have been mutated was measured by indirect ELISA and competitive ELISA.
For the majority of the patients, mutation reduced significantly IgE-binding but did not suppress it completely. Thus, most of the patients likely produce IgE directed against epitopes, until now, considered as minor. Nevertheless, we observed a great variability in patient responses. For some patients, the complete suppression of IgE-binding was achieved.
Such recombinant mutated αS1-caseins with reduced IgE-binding ability can be useful for the development of CMA immunotherapy.
This article is published under license to BioMed Central Ltd. This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.