%0 Journal Article
%A San Segundo Acosta, Pablo
%A Oeo Santos, Carmen
%A Benedé Pérez, Sara
%A de los Ríos, Vivian
%A Navas, Ana
%A Ruiz Leon, Berta
%A Moreno, Carmen
%A Pastor Vargas, Carlos
%A Jurado, Aurora
%A Villalba, Mayte
%A Villalba Díaz, María Teresa
%A Barderas Manchado, Rodrigo
%T Delineation of the olive pollen proteome and its allergenome unmasks cyclophilin as a relevant cross-reactive allergen
%D 2019
%@ 1535-3893
%@ 1535-3907
%U https://hdl.handle.net/20.500.14352/109596
%X Olive 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.
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