The amino acid sequence of Ole e I, the major allergen from olive tree (Olea europaea) pollen (original) (raw)
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The Journal of biological chemistry, 1994
Ole e I, the major allergen from the olive tree (Olea europaea), is one of the main causes of allergy in Mediterranean countries and some areas of North America. The cloning and sequencing of several cDNAs coding for the olive allergen have been achieved. cDNA has been synthesized from total pollen RNA and amplified by using the polymerase chain reaction. The nucleotide sequence data demonstrate the existence of microheterogeneities in at least 37 positions out of the 145 amino acids of Ole e I, thus explaining the high degree of polymorphism exhibited by the natural protein. One of the sequenced cDNAs encoding a full-length isoform was inserted into the plasmid vector pGEX-2T and overexpressed. The recombinant Ole e I has been produced in Escherichia coli as a fusion protein with glutathione S-transferase of Schistosoma japonicum. This chimeric protein was purified by affinity chromatography on a glutathione-Sepharose 4B column and digested with thrombin to release the recombinant ...
Purification and fine characterization of a major allergen from Olea europaea pollen extract
Allergy, 1993
Olea europaea (olive) pollen extract was prepared by aqueous extraction and characterized by biochemical and immunochemical methods. Two components, displaying respective mol. wt. of 17000 and 19000, were the most reactive allergens, being the doublet (designated Ole e I) recognized by most sera tested. The 19000 mol. wt. component, purified by conventional biochemical procedure and lectin-affinity chromatography from the Ole e I doublet, was deglycosylated and analyzed by SDS–PAGE and by ELISA inhibition. The results obtained suggest that the 19000 mol. wt. component represents the glycosylated form of the 17000 component.