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.
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: Lesa R Offermann; Caleb R Schlachter; Makenzie L Perdue; Karolina A Majorek; John Z He; William T Booth; Jessica Garrett; Krzysztof Kowal; Maksymilian Chruszcz Journal: J Biol Chem Date: 2016-05-26 Impact factor: 5.157
Authors: A Brenda Kapingidza; Sarah E Pye; Noah Hyduke; Coleman Dolamore; Swanandi Pote; Caleb R Schlachter; Scott P Commins; Krzysztof Kowal; Maksymilian Chruszcz Journal: Mol Immunol Date: 2019-07-18 Impact factor: 4.407
Authors: Michael W Handlogten; Tanyel Kiziltepe; Ana P Serezani; Mark H Kaplan; Basar Bilgicer Journal: Nat Chem Biol Date: 2013-10-06 Impact factor: 15.040