Publication: Delineation of the Olive Pollen Proteome and Its Allergenome Unmasks Cyclophilin as a Relevant Cross-Reactive Allergen.
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Date
2019-06-27
Authors
San Segundo-Acosta, Pablo
Oeo-Santos, Carmen
Benedé, Sara
de Los Ríos, Vivian
Navas, Ana
Ruiz-Leon, Berta
Moreno, Carmen
Pastor-Vargas, Carlos
Jurado, Aurora
Villalba, Mayte
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Abstract
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.
Description
MeSH Terms
Allergens
Amino Acid Sequence
Animals
Antigens, Plant
Child
Chromatography, Liquid
Cross Reactions
Cyclophilins
Humans
Immunoglobulin E
Olea
Pollen
Proteome
Proteomics
Tandem Mass Spectrometry
Amino Acid Sequence
Animals
Antigens, Plant
Child
Chromatography, Liquid
Cross Reactions
Cyclophilins
Humans
Immunoglobulin E
Olea
Pollen
Proteome
Proteomics
Tandem Mass Spectrometry
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Keywords
allergen, allergenome, cross-reactivity, cyclophilin, in-depth proteomics, olive pollen proteome