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An experimental and modeling-based approach to locate IgE epitopes of plant profilin allergens.
J Allergy Clin Immunol. 2007 Jun; 119(6):1481-8.JA

Abstract

BACKGROUND

Plant profilins are actin-binding proteins that form a well-known panallergen family responsible for cross-sensitization between plant foods and pollens. Melon profilin, Cuc m 2, is the major allergen of this fruit.

OBJECTIVE

We sought to map IgE epitopes on the 3-dimensional structure of Cuc m 2.

METHODS

IgE binding to synthetic peptides spanning the full Cuc m 2 amino acid sequence was assayed by using a serum pool and individual sera from 10 patients with melon allergy with significant specific IgE levels to this allergen. Three-dimensional modeling and potential epitope location were based on analysis of both solvent exposure and electrostatic properties of the Cuc m 2 surface.

RESULTS

Residues included in synthetic peptides that exerted the strongest IgE-binding capacity defined 2 major epitopes (E1, consisting of residues 66-75 and 81-93, and E2, consisting of residues 95-99 and 122-131) that partially overlapped with the actin-binding site of Cuc m 2. Two additional epitopes (E3, including residues 2-10, and E4, including residues 35-45) that should show weaker putative antigen-antibody associations and shared most residues with synthetic peptides with low IgE-binding capacity were predicted on theoretical grounds.

CONCLUSIONS

Strong and weak IgE epitopes have been uncovered in melon profilin, Cuc m 2.

CLINICAL IMPLICATIONS

The different types of IgE epitopes located in the 3-dimensional structure of melon profilin can constitute the molecular basis to explain the sensitization and cross-reactivity exhibited by this panallergen family.

Authors+Show Affiliations

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

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

17397911

Citation

López-Torrejón, Gema, et al. "An Experimental and Modeling-based Approach to Locate IgE Epitopes of Plant Profilin Allergens." The Journal of Allergy and Clinical Immunology, vol. 119, no. 6, 2007, pp. 1481-8.
López-Torrejón G, Díaz-Perales A, Rodríguez J, et al. An experimental and modeling-based approach to locate IgE epitopes of plant profilin allergens. J Allergy Clin Immunol. 2007;119(6):1481-8.
López-Torrejón, G., Díaz-Perales, A., Rodríguez, J., Sánchez-Monge, R., Crespo, J. F., Salcedo, G., & Pacios, L. F. (2007). An experimental and modeling-based approach to locate IgE epitopes of plant profilin allergens. The Journal of Allergy and Clinical Immunology, 119(6), 1481-8.
López-Torrejón G, et al. An Experimental and Modeling-based Approach to Locate IgE Epitopes of Plant Profilin Allergens. J Allergy Clin Immunol. 2007;119(6):1481-8. PubMed PMID: 17397911.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - An experimental and modeling-based approach to locate IgE epitopes of plant profilin allergens. AU - López-Torrejón,Gema, AU - Díaz-Perales,Araceli, AU - Rodríguez,Julia, AU - Sánchez-Monge,Rosa, AU - Crespo,Jesus F, AU - Salcedo,Gabriel, AU - Pacios,Luis F, Y1 - 2007/03/30/ PY - 2007/01/03/received PY - 2007/01/30/revised PY - 2007/02/07/accepted PY - 2007/4/3/pubmed PY - 2007/7/28/medline PY - 2007/4/3/entrez SP - 1481 EP - 8 JF - The Journal of allergy and clinical immunology JO - J Allergy Clin Immunol VL - 119 IS - 6 N2 - BACKGROUND: Plant profilins are actin-binding proteins that form a well-known panallergen family responsible for cross-sensitization between plant foods and pollens. Melon profilin, Cuc m 2, is the major allergen of this fruit. OBJECTIVE: We sought to map IgE epitopes on the 3-dimensional structure of Cuc m 2. METHODS: IgE binding to synthetic peptides spanning the full Cuc m 2 amino acid sequence was assayed by using a serum pool and individual sera from 10 patients with melon allergy with significant specific IgE levels to this allergen. Three-dimensional modeling and potential epitope location were based on analysis of both solvent exposure and electrostatic properties of the Cuc m 2 surface. RESULTS: Residues included in synthetic peptides that exerted the strongest IgE-binding capacity defined 2 major epitopes (E1, consisting of residues 66-75 and 81-93, and E2, consisting of residues 95-99 and 122-131) that partially overlapped with the actin-binding site of Cuc m 2. Two additional epitopes (E3, including residues 2-10, and E4, including residues 35-45) that should show weaker putative antigen-antibody associations and shared most residues with synthetic peptides with low IgE-binding capacity were predicted on theoretical grounds. CONCLUSIONS: Strong and weak IgE epitopes have been uncovered in melon profilin, Cuc m 2. CLINICAL IMPLICATIONS: The different types of IgE epitopes located in the 3-dimensional structure of melon profilin can constitute the molecular basis to explain the sensitization and cross-reactivity exhibited by this panallergen family. SN - 0091-6749 UR - https://www.unboundmedicine.com/medline/citation/17397911/An_experimental_and_modeling_based_approach_to_locate_IgE_epitopes_of_plant_profilin_allergens_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0091-6749(07)00362-4 DB - PRIME DP - Unbound Medicine ER -