IlTriEmor1
Ontology highlight
ABSTRACT:
PROVIDER: PRJEB56843 | ENA |
REPOSITORIES: ENA
Similar Datasets
Project description:Trisateles emortualis (olive crescent) genome assembly, ilTriEmor1, alternate haplotype
| PRJEB56842 | ENA
Project description:Trisateles emortualis (olive crescent), genomic and transcriptomic data
| PRJEB55138 | ENA
Project description:Teleiodes luculella (crescent groundling) genome assembly, ilTelLucu1
| PRJEB59316 | ENA
Project description:Epinotia bilunana (crescent bell) genome assembly, ilEpiBilu1
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Project description:Marasmarcha lunaedactyla (crescent plume) genome assembly, ilMarLuna1
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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 | PXD012280 | Pride
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 | PXD012279 | Pride