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Mimotope mapping as a complementary strategy to define allergen IgE-epitopes: peach Pru p 3 allergen as a model.
Mol Immunol. 2008 Apr; 45(8):2269-76.MI

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.

Authors+Show Affiliations

Unidad de Química y Bioquímica, Departamento de Biotecnología, E.T.S. Ingenieros de Montes, Madrid, Spain.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article

Language

eng

PubMed ID

18242709

Citation

Pacios, Luis F., et al. "Mimotope Mapping as a Complementary Strategy to Define Allergen IgE-epitopes: Peach Pru P 3 Allergen as a Model." Molecular Immunology, vol. 45, no. 8, 2008, pp. 2269-76.
Pacios LF, Tordesillas L, Cuesta-Herranz J, et al. Mimotope mapping as a complementary strategy to define allergen IgE-epitopes: peach Pru p 3 allergen as a model. Mol Immunol. 2008;45(8):2269-76.
Pacios, L. F., Tordesillas, L., Cuesta-Herranz, J., Compes, E., Sánchez-Monge, R., Palacín, A., Salcedo, G., & Díaz-Perales, A. (2008). Mimotope mapping as a complementary strategy to define allergen IgE-epitopes: peach Pru p 3 allergen as a model. Molecular Immunology, 45(8), 2269-76. https://doi.org/10.1016/j.molimm.2007.11.022
Pacios LF, et al. Mimotope Mapping as a Complementary Strategy to Define Allergen IgE-epitopes: Peach Pru P 3 Allergen as a Model. Mol Immunol. 2008;45(8):2269-76. PubMed PMID: 18242709.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Mimotope mapping as a complementary strategy to define allergen IgE-epitopes: peach Pru p 3 allergen as a model. AU - Pacios,Luis F, AU - Tordesillas,Leticia, AU - Cuesta-Herranz,Javier, AU - Compes,Esther, AU - Sánchez-Monge,Rosa, AU - Palacín,Arantxa, AU - Salcedo,Gabriel, AU - Díaz-Perales,Araceli, Y1 - 2008/02/01/ PY - 2007/09/13/received PY - 2007/11/21/accepted PY - 2008/2/5/pubmed PY - 2008/6/6/medline PY - 2008/2/5/entrez SP - 2269 EP - 76 JF - Molecular immunology JO - Mol Immunol VL - 45 IS - 8 N2 - 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. SN - 0161-5890 UR - https://www.unboundmedicine.com/medline/citation/18242709/Mimotope_mapping_as_a_complementary_strategy_to_define_allergen_IgE_epitopes:_peach_Pru_p_3_allergen_as_a_model_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0161-5890(07)00856-5 DB - PRIME DP - Unbound Medicine ER -