Project description:Proteins and peptides are minor components of vegetal oils. The presence of these compounds in virgin olive oil was first reported in 2001, but the nature of the olive oil proteome is still a puzzling question for food science researchers. In this project, we have compiled for a first time a comprehensive proteomic dataset of olive fruit and fungal proteins that are present at low but measurable concentrations in a vegetable oil from a crop of great agronomical relevance as olive (Olea europaea L.). Accurate mass nLC-MS data were collected in high definition direct data analysis (HD-DDA) mode using the ion mobility separation step. Protein identification was performed using the Mascot Server v2.2.07 software (Matrix Science) against an ad hoc database made of olive protein entries. Starting from this proteomic record, the impact of these proteins on olive oil stability and quality could be tested. Moreover, the effect of olive oil proteins on human health and their potential use as functional food components could be also evaluated. In addition, this dataset provides a resource for use in further functional comparisons across other vegetable oils, and also expands the proteomic resources to non-model species, thus also allowing further comparative inter-species studies.

2020-09-29 | PXD019894 | Pride

Delineation of the olive pollen proteome: A focus on its allergen families reveals cyclophilin as a relevant allergen, part 2

Project description:The delineation of the olive pollen proteome and its allergogram can improve the clinical management of patients with this pollinosis. We here integrated the recently described wild olive genomic data in a comprehensive proteomic approach to get the annotated olive (Olea europaea) pollen proteome and complete its complex allergogram. Olive pollen proteins were identified by LC-MS/MS using predicted protein sequences from its genome. GO annotation, KEGG Pathway analysis and identification of allergen families were performed by bioinformatics. Recombinant DNA, protein expression and purification, and immunological analyses were used to characterize putative allergens. A total of 1,907 proteins were identified. 60% of the proteins were predicted to possess catalytic activity and be involved in metabolic processes. 203 proteins belonging to 47 allergen families were found, with 37 non-previously described in olive pollen. Of four potential allergens produced in Escherichia coli, a peptidyl-prolyl cis-trans isomerase -cyclophilin-, masked in the protein extract by the major allergen Ole e 1, was found as a new olive pollen allergen (Ole e 15). 63% of the Ole e 15-sensitized patients were children and showed strong IgE recognition of the allergen. Ole e 15 shared high sequence identity with other plant, animal and fungal cyclophilins and a high IgE cross-reactivity with pollen, plant food and animal extracts. Taken together, the combination of available genomic data with proteomics permitted the profiling of the olive pollen proteome, revealing the spectrum of allergen families and cyclophilin as a new relevant allergen implicated in cross-reactivity.

2019-06-17 | PXD012334 | Pride

Delineation of the olive pollen proteome: A focus on its allergen families reveals cyclophilin as a relevant allergen

2019-06-17 | PXD012280 | Pride