Mimotope mapping as a complementary strategy to define allergen IgE-epitopes: peach Pru p 3 allergen as a model.

Pacios, Luis F. and Tordesillas Villuendas, Leticia and Cuesta-Herranz, Javier and Compes, Esther and Sánchez-Monge Laguna de Rins, Rosa and Palacín Gómez, Aranzazu and Salcedo Duran, Gabriel and Díaz Perales, Araceli (2008). Mimotope mapping as a complementary strategy to define allergen IgE-epitopes: peach Pru p 3 allergen as a model.. "Molecular Immunology", v. 45 (n. 8); pp. 2269-2276. ISSN 0161-5890. https://doi.org/10.1016/j.molimm.2007.11.022.

Description

Title: Mimotope mapping as a complementary strategy to define allergen IgE-epitopes: peach Pru p 3 allergen as a model.
Author/s:
  • Pacios, Luis F.
  • Tordesillas Villuendas, Leticia
  • Cuesta-Herranz, Javier
  • Compes, Esther
  • Sánchez-Monge Laguna de Rins, Rosa
  • Palacín Gómez, Aranzazu
  • Salcedo Duran, Gabriel
  • Díaz Perales, Araceli
Item Type: Article
Título de Revista/Publicación: Molecular Immunology
Date: April 2008
ISSN: 0161-5890
Volume: 45
Subjects:
Freetext Keywords: Lipid transfer protein; Pru p 3; Mimotopes; IgE-epitope; 3D modelling; Solvent exposure; Electrostatic potential; Allergen surface
Faculty: E.T.S.I. Agrónomos (UPM) [antigua denominación]
Department: Biotecnologia [hasta 2014]
Creative Commons Licenses: Recognition - No derivative works - Non commercial

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Abstract

Lipid transfer proteins (LTPs) are the major allergens of Rosaceae fruits in the Mediterranean area. Pru p 3, the LTP and major allergen of peach, is a suitable model for studying food allergy and amino acid sequences related with its IgE-binding capacity. In this work, we sought to map IgE mimotopes on the structure of Pru p 3, using the combination of a random peptide phage display library and a three-dimensional modelling approach. Pru p 3-specific IgE was purified from 2 different pools of sera from peach allergic patients grouped by symptoms (OAS-pool or SYS-pool), and used for screening of a random dodecapeptide phage display library. Positive clones were further confirmed by ELISA assays testing individual sera from each pool. Three-dimensional modelling allowed location of mimotopes based on analysis of electrostatic properties and solvent exposure of the Pru p 3 surface. Twenty-one phage clones were selected using Pru p 3-specific IgE, 9 of which were chosen using OAS-specific IgE while the other 12 were selected with systemic-specific IgE. Peptide alignments revealed consensus sequences for each pool: L37 R39 T40 P42 D43 R44 A46 P70 S76 P78 Y79 for OAS-IgE, and N35 N36 L37 R39 T40 D43 A46 S76 I77 P78 for systemic-IgE. These 2 consensus sequences were mapped on the same surface of Pru p 3, corresponding to the helix 2-loop-helix 3 region and part of the non-structured C-terminal coil. Thus, 2 relevant conformational IgE-binding regions of Pru p 3 were identified using a random peptide phage display library. Mimotopes can be used to study the interaction between allergens and IgE, and to accelerate the process to design new vaccines and new immunotherapy strategies

More information

Item ID: 2248
DC Identifier: https://oa.upm.es/2248/
OAI Identifier: oai:oa.upm.es:2248
DOI: 10.1016/j.molimm.2007.11.022
Official URL: http://www.sciencedirect.com/science?_ob=Publicati...
Deposited by: Memoria Investigacion
Deposited on: 17 Feb 2010 10:01
Last Modified: 20 Apr 2016 11:59
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