PURIFICATION, AMINO-ACID-SEQUENCE AND IMMUNOLOGICAL CHARACTERIZATION OF OLE-E-6, A CYSTEINE-ENRICHED ALLERGEN FROM OLIVE TREE POLLEN

The Ole e 6 allergen from olive tree pollen has been isolated by combi ning gel permeation and reverse-phase chromatographies, It is a single and highly acidic (pI 4.2) polypeptide chain protein, Its NH2-termina l amino acid sequence has been determined by Edman degradation, Total RNA from the olive tree pollen was isolated, and a specific cDNA was a mplified by the polymerase chain reaction using a degenerate oligonucl eotide primer designed according to the NH2-terminal sequence of the p rotein, The nucleotide sequencing of the cDNA rendered an open reading frame encoding a 50 amino acid polypeptide chain, in which two sets o f the sequential motif Cys-X-3-Cys-X-3-Cys are present, No sequence si milarity has been found between this protein and other previously desc ribed polypeptides. (C) 1997 Federation of European Biochemical Societ ies.