Epitopes described in "Cloning, expression, and mapping of allergenic determinants of alphaS1-casein, a major cow's milk allergen."

Article Authors:Ulrike Schulmeister; Heidrun Hochwallner; Ines Swoboda; Margarete Focke-Tejkl; Beate Geller; Mats Nystrand; Annika Härlin; Josef Thalhamer; Sandra Scheiblhofer; Walter Keller; Bodo Niggemann; Santiago Quirce; Christoph Ebner; Adriano Mari; Gabrielle Pauli; Udo Herz; Rudolf Valenta; Susanne Spitzauer
Article Title:Cloning, expression, and mapping of allergenic determinants of alphaS1-casein, a major cow's milk allergen.
Reference Detail
Reference ID:1014862
Abstract:Milk is one of the first components introduced into human diet. It also represents one of the first allergen sources, which induces IgE-mediated allergies in childhood ranging from gastrointestinal, skin, and respiratory manifestations to severe life-threatening manifestations, such as anaphylaxis. Here we isolated a cDNA coding for a major cow's milk allergen, alphaS1-casein, from a bovine mammary gland cDNA library with allergic patients' IgE Abs. Recombinant alphaS1-casein was expressed in Escherichia coli, purified, and characterized by circular dichroism as a folded protein. IgE epitopes of alphaS1-casein were determined with recombinant fragments and synthetic peptides spanning the alphaS1-casein sequence using microarrayed components and sera from 66 cow's milk-sensitized patients. The allergenic activity of ralphaS1-casein and the alphaS1-casein-derived peptides was determined using rat basophil leukemia cells transfected with human FcepsilonRI, which had been loaded with the patients' serum IgE. Our results demonstrate that ralphaS1-casein as well as alphaS1-casein-derived peptides exhibit IgE reactivity, but mainly the intact ralphaS1-casein induced strong basophil degranulation. These results suggest that primarily intact alphaS1-casein or larger IgE-reactive portions thereof are responsible for IgE-mediated symptoms of food allergy. Recombinant alphaS1-casein as well as alphaS1-casein-derived peptides may be used in clinical studies to further explore pathomechanisms of food allergy as well as for the development of new diagnostic and therapeutic strategies for milk allergy.
Affiliations:Institute of Medical and Chemical Laboratory Diagnostics, Medical University of Vienna, Austria.
Reference Type:Literature
PubMed ID:19454699
Journal:J Immunol
Journal Volume:182
Article Pages:7019-29
Journal ISSN:1550-6606
Article Chemical List:Allergens;Caseins;DNA, Complementary;Epitopes;Peptide Fragments;Receptors, IgE;Immunoglobulin E
Article MeSH List:Allergens(immunology); Animals; Basophils(physiology); Caseins(immunology); Cattle; Cell Degranulation; Cell Line, Tumor; Cloning, Molecular; DNA, Complementary; Epitope Mapping; Epitopes(genetics; immunology); Humans; Immunoglobulin E; Milk(immunology); Milk Hypersensitivity(immunology); Peptide Fragments(chemical synthesis; immunology); Rats; Receptors, IgE
Curation Last Updated:2014-10-03 21:34:13