Monovalent fusion proteins of IgE mimotopes are safe for therapy of type I allergy

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 f...

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Bibliographic Details
Published in:The FASEB journal 2001-11, Vol.15 (13), p.2524-2526
Main Authors: Ganglberger, E, Barbara Sponer, Schöll, I, Wiedermann, U, Baumann, S, Hafner, C, Breiteneder, H, Suter, M, Boltz-Nitulescu, G, Scheiner, O, Jensen-Jarolim, E
Format: Article
Language:English
Subjects:
Allergens
Amino Acid Sequence
Animals
Antibodies - blood
Antibody Formation
Antigens, Plant
Contractile Proteins
Epitopes - genetics
Epitopes - immunology
Humans
Hypersensitivity - immunology
Immunoglobulin E - genetics
Immunoglobulin E - immunology
Immunoglobulin G - blood
Immunotherapy
Mice
Mice, Inbred BALB C
Microfilament Proteins - genetics
Microfilament Proteins - immunology
Molecular Mimicry - genetics
Molecular Mimicry - immunology
Plant Proteins - immunology
Plasmids - genetics
Profilins
Receptors, Albumin - genetics
Recombinant Fusion Proteins - genetics
Recombinant Fusion Proteins - immunology
Skin Tests
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Summary: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.
ISSN:0892-6638
1530-6860
DOI:10.1096/fj.00-0888fje