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Descripción
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| 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. | |
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Internacional
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No |
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JCR del ISI
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No |
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Título de la revista
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J Allergy Clin Immunol. |
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ISSN
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17397911 |
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Factor de impacto JCR
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0 |
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Información de impacto
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Volumen
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119 |
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DOI
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Número de revista
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6 |
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Desde la página
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1481 |
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Hasta la página
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1488 |
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JUNIO |
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