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Monovalent fusion proteins of immunoglobulin E mimotopes are safe for therapy of type I allergy
Author(s) -
Ganglberger E.,
Sponer B.,
Schöll I.,
Wiedermann U.,
Baumann S.,
Hafner C.,
Breiteneder H.,
Suter M.,
Boltz-Nitulescu G.,
Scheiner O.,
Jensen-Jarolim E.
Publication year - 2001
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fj.00-0888fje
Subject(s) - mimotope , epitope , immunoglobulin e , antibody , fusion protein , immunology , immunotherapy , chemistry , biology , recombinant dna , immune system , biochemistry , gene
By screening phage display random peptide libraries with purified immunoglobulin E (IgE) from birch pollen‐allergic patients, we previously defined peptides mimicking natural IgE epitopes (mimotopes) of the major birch pollen allergen Bet v 1. The present study aimed to define a monovalent carrier for the IgE mimotopes to induce protective antibodies directed to the IgE epitopes, suitable for mimotope‐specific therapy. We expressed the selected mimotopes as fusion proteins together with streptococcal albumin binding protein (ABP). The fusion proteins were recognized specifically by anti ‐Bet v 1 human IgE, which demonstrated that the mimotopes fused to ABP resemble the natural IgE epitope. Bet v 1‐specific IgG was induced by immunization of BALB/c mice with fusion proteins. These IgG antibodies could inhibit IgE binding to Bet v 1. Skin testing of Bet v 1 allergic mice showed that the ABP mimotope constructs did not elicit type I skin reactions, although they possess IgE binding structures. Our data suggest that IgE mimotopes are safe for epitope‐specific immunotherapy of sensitized individuals, when presented in a monovalent form. Therefore, ABP‐fused mimotopes are promising candidates for a new type of immunotherapy based on the precise induction of blocking antibodies.