These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: An experimental and modeling-based approach to locate IgE epitopes of plant profilin allergens.
    Author: López-Torrejón G, Díaz-Perales A, Rodríguez J, Sánchez-Monge R, Crespo JF, Salcedo G, Pacios LF.
    Journal: J Allergy Clin Immunol; 2007 Jun; 119(6):1481-8. PubMed ID: 17397911.
    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.
    [Abstract] [Full Text] [Related] [New Search]