Table of Contents Author Guidelines Submit a Manuscript
Clinical and Developmental Immunology
Volume 2013, Article ID 385615, 12 pages
http://dx.doi.org/10.1155/2013/385615
Research Article

Allergenic Characterization of New Mutant Forms of Pru p 3 as New Immunotherapy Vaccines

1Centro de Biotecnología y Genómica de Plantas (UPM-INIA), Campus de Montegancedo, Pozuelo de Alarcón, 28223 Madrid, Spain
2Servicio de Alergia, Hospital de Basurto, Bilbao, Spain
3Servicio de Alergia, Hospital Infanta Leonor, Madrid, Spain
4Servicio de Quimica de Proteinas, Centro de Investigaciones Biologicas, CSIC, Madrid, Spain
5IIS-Servicio de Alergia, Fundación Jiménez Díaz, Madrid, Spain
6Departamento de Biotecnología, E.T.S. Ingenieros de Montes, UPM, Madrid, Spain

Received 23 July 2013; Accepted 12 September 2013

Academic Editor: Pedro A. Reche

Copyright © 2013 C. Gómez-Casado et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Abstract

Nowadays, treatment of food allergy only considered the avoidance of the specific food. However, the possibility of cross-reactivity makes this practice not very effective. Immunotherapy may exhibit as a good alternative to food allergy treatment. The use of hypoallergenic molecules with reduced IgE binding capacity but with ability to stimulate the immune system is a promising tool which could be developed for immunotherapy. In this study, three mutants of Pru p 3, the principal allergen of peach, were produced based on the described mimotope and T cell epitopes, by changing the specific residues to alanine, named as Pru p 3.01, Pru p 3.02, and Pru p 3.03. Pru p 3.01 showed very similar allergenic activity as the wild type by in vitro assays. However, Pru p 3.02 and Pru p 3.03 presented reduced IgE binding with respect to the native form, by in vitro, ex vivo, and in vivo assays. In addition, Pru p 3.03 had affected the IgG4 binding capacity and presented a random circular dichroism, which was reflected in the nonrecognition by specific antibodies anti-Pru p 3. Nevertheless, both Pru p 3.02 and Pru p 3.03 maintained the binding to IgG1 and their ability to activate T lymphocytes. Thus, Pru p 3.02 and Pru p 3.03 could be good candidates for potential immunotherapy in peach-allergic patients.