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Prevention of allergy by a recombinant multi-allergen vaccine with reduced IgE binding and preserved T cell epitopes

Karamloo, Fariba and Schmid-Grendelmeier, Peter and Kussebi, Fatimah and Akdis, Mübeccel and Salagianni, Maria and von Beust, Barbara R. and Reimers, Andrea and Zumkehr, Judith and Soldatova, Lyudmilla and Housley-Markovic, Zora and Müller, Ulrich and Kündig, Thomas and Kemeny, David M. and Spangfort, Michael D. and Blaser, Kurt and Akdis, Cezmi A.. (2005) Prevention of allergy by a recombinant multi-allergen vaccine with reduced IgE binding and preserved T cell epitopes. European Journal of Immunology, Vol. 35, H. 11. S. 3268-3276.

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Official URL: http://edoc.unibas.ch/dok/A5258243

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Abstract

Novel approaches for the prevention of allergy are required, because of the inevitably increasing prevalence of allergic diseases during the last 30 years. Here, a recombinant chimeric protein, which comprises the whole amino acid sequences of three bee venom major allergens has been engineered and used in prevention of bee venom sensitization in mice. Phospholipase A2 (Api m 1), hyaluronidase (Api m 2) and melittin (Api m 3) fragments with overlapping amino acids were assembled in a different order in the Api m (1/2/3) chimeric protein, which preserved entire T cell epitopes, whereas B cell epitopes of all three allergens were abrogated. Accordingly, IgE cross-linking leading to mast cell and basophil mediator release was profoundly reduced in humans. Supporting these findings, the Api m (1/2/3) induced 100 to 1000 times less type-1 skin test reactivity in allergic patients. Treatment of mice with Api m (1/2/3) led to a significant reduction of specific IgE development towards native allergen, representing a protective vaccine effect in vivo. These results demonstrate a novel prototype of a preventive allergy vaccine, which preserves the entire T cell epitope repertoire, but bypasses induction of IgE against native allergen, and side effects related to mast cell/basophil IgE FcepsilonRI cross-linking in sensitized individuals.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Structural Biology & Biophysics > Structural Biology (Schirmer)
UniBasel Contributors:Schirmer, Tilman
Item Type:Article, refereed
Bibsysno:Link to catalogue
Publisher:Verl. Chemie
ISSN:0014-2980
Note:Publication type according to Uni Basel Research Database: Journal article
Last Modified:07 Aug 2015 12:05
Deposited On:22 Mar 2012 13:20

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