San Segundo-Acosta, PabloOeo-Santos, CarmenNavas, AnaJurado, AuroraVillalba, MayteBarderas, Rodrigo2024-01-232024-01-232019San Segundo-Acosta, P., Oeo-Santos, C., Navas, A. et al. Ole e 15 and its human counterpart -PPIA- chimeras reveal an heterogeneous IgE response in olive pollen allergic patients. Sci Rep 9, 15027 (2019). https://doi.org/10.1038/s41598-019-51005-22045-2322https://hdl.handle.net/10115/28722Olive pollen is a major cause of immunoglobulin E (IgE)-mediated allergy in Mediterranean countries. It is expected to become a worldwide leading allergenic source because olive cultivation is increasing in many countries. Ole e 15 belongs to the cyclophilin pan-allergen family, which includes highly cross-reactive allergens from non-related plant, animal and mold species. Here, the amino acid differences between Ole e 15 and its weak cross-reactive human homolog PPIA were grafted onto Ole e 15 to assess the contribution of specific surface areas to the IgE-binding. Eight Ole e 15-PPIA chimeras were produced in E. coli, purified and tested with 20 sera from Ole e 15-sensitized patients with olive pollen allergy by ELISA experiments. The contribution of linear epitopes was analyzed using twelve overlapping peptides spanning the entire Ole e 15 sequence. All the patients displayed a diverse reduction of the IgE-reactivity to the chimeras, revealing a highly polyclonal and patient-specific response to Ole e 15. IgE-epitopes are distributed across the entire Ole e 15 surface. Two main surface areas containing relevant conformational epitopes have been characterized. This is the first study to identify important IgE-binding regions on the surface of an allergenic cyclophilin.engAttribution 4.0 Internationalhttps://creativecommons.org/licenses/by/4.0/Olive pollen allergy, cross-reactivity, cyclophilinOle e 15 and its human counterpart -PPIA- chimeras reveal an heterogeneous IgE response in olive pollen allergic patientsinfo:eu-repo/semantics/article10.1038/s41598-019-51005-2.info:eu-repo/semantics/restrictedAccess