San Segundo-Acosta, PabloOeo-Santos, CarmenBenedé, Sarade Los Ríos, VivianNavas, AnaRuíz-León, BertaMoreno-Aguilar, CarmenPastor-Vargas, CarlosJurado, AuroraVillalba, MayteBarderas, Rodrigo2024-01-232024-01-2320191535-3893https://hdl.handle.net/10115/28723Olive 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.engOlive pollen proteome, allergenome, in-depth proteomics, allergen, cyclophilin, cross-reactivityinfo:eu-repo/semantics/article10.1021/acs.jproteome.9b00167info:eu-repo/semantics/restrictedAccess