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Delineation of the olive pollen proteome and its allergenome unmasks cyclophilin as a relevant cross-reactive allergen

AuthorsSan Segundo-Acosta, Pablo; Oeo-Santos, Carmen; Benedé, Sara ; Ríos, Vivian de los ; Navas, Ana; Ruiz-León, Berta; Moreno, Carmen; Pastor-Vargas, Carlos; Jurado, Aurora; Villalba, Mayte; Barderas, Rodrigo
In-depth proteomics
Olive pollen proteome
Issue Date27-Jun-2019
PublisherAmerican Chemical Society
CitationJ. Proteome Res (2019)
AbstractOlive 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.
Description37 p.-5 fig.-1 tab.
Publisher version (URL)https://doi.org/10.1021/acs.jproteome.9b00167
Appears in Collections:(CIB) Artículos
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