| Literature DB >> 31192604 |
Pablo San Segundo-Acosta1, Carmen Oeo-Santos1, Sara Benedé1, Vivian de Los Ríos2, Ana Navas3, Berta Ruiz-Leon3, Carmen Moreno3, Carlos Pastor-Vargas4, Aurora Jurado3, Mayte Villalba1, Rodrigo Barderas5.
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.Entities:
Keywords: allergen; allergenome; cross-reactivity; cyclophilin; in-depth proteomics; olive pollen proteome
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Year: 2019 PMID: 31192604 DOI: 10.1021/acs.jproteome.9b00167
Source DB: PubMed Journal: J Proteome Res ISSN: 1535-3893 Impact factor: 4.466