San Segundo-Acosta, PabloOeo-Santos, CarmenBenedé, Sarade Los Ríos, VivianNavas, AnaRuiz-Leon, BertaMoreno, CarmenPastor-Vargas, CarlosJurado, AuroraVillalba, MayteBarderas, Rodrigo2023-01-252023-01-252019-06-27http://hdl.handle.net/10668/14103Olive pollen is a major allergenic source worldwide due to its extensive cultivation. We have combined available genomics data with a comprehensive proteomics approach to get the annotated olive tree (Olea europaea L.) pollen proteome and define its complex allergenome. A total of 1907 proteins were identified by LC-MS/MS using predicted protein sequences from its genome. Most proteins (60%) were predicted to possess catalytic activity and be involved in metabolic processes. In total, 203 proteins belonging to 47 allergen families were found in olive pollen. A peptidyl-prolyl cis-trans isomerase, cyclophilin, produced in Escherichia coli, was found as a new olive pollen allergen (Ole e 15). Most Ole e 15-sensitized patients were children (63%) and showed strong IgE recognition to the allergen. Ole e 15 shared high sequence identity with other plant, animal, and fungal cyclophilins and presented high IgE cross-reactivity with pollen, plant food, and animal extracts.enallergenallergenomecross-reactivitycyclophilinin-depth proteomicsolive pollen proteomeAllergensAmino Acid SequenceAnimalsAntigens, PlantChildChromatography, LiquidCross ReactionsCyclophilinsHumansImmunoglobulin EOleaPollenProteomeProteomicsTandem Mass Spectrometryresearch article31192604open access10.1021/acs.jproteome.9b001671535-3907https://digital.csic.es/bitstream/10261/186354/3/JPR_San%20Segundo-Acosta_2019.pdf