%0 Journal Article
%A San Segundo-Acosta, Pablo
%A Oeo-Santos, Carmen
%A Benedé, 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 Barderas, Rodrigo
%T Delineation of the Olive Pollen Proteome and Its Allergenome Unmasks Cyclophilin as a Relevant Cross-Reactive Allergen.
%D 2019
%U http://hdl.handle.net/10668/14103
%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.
%K allergen
%K allergenome
%K cross-reactivity
%K cyclophilin
%K in-depth proteomics
%K olive pollen proteome
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