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 combining gel permeation and reverse-phase chromatographies. It is a single and highly acidic (pI 4.2) polypeptide chain protein. Its NH2-terminal amino acid sequence has been determined by Edman degradation. Total RNA from the olive tree pollen was isolated, and a specific cDNA was amplified by the polymerase chain reaction using a degenerate oligonucleotide primer designed according to the NH2-terminal sequence of the protein. The nucleotide sequencing of the cDNA rendered an open reading frame encoding a 50 amino acid polypeptide chain, in which two sets of the sequential motif Cys-X3-Cys-X3-Cys are present. No sequence similarity has been found between this protein and other previously described polypeptides.
Batanero
E
E
Departamento de Bioquímica y Biologia Molecular, Facultad de Química,Universidad Complutense, Madrid, Spain.
Ledesma
A
A
Villalba
M
M
Rodríguez
R
R
D000485:Allergens / Q000737:chemistry / Q000235:genetics / Q000276:immunology / Q000302:isolation & purification*; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D018076:DNA, Complementary; D006801:Humans; D007073:Immunoglobulin E / Q000276:immunology; D008969:Molecular Sequence Data; D010940:Plant Proteins / Q000737:chemistry / Q000235:genetics / Q000276:immunology / Q000302:isolation & purification*; D011058:Pollen; D011817:Rabbits; D017386:Sequence Homology, Amino Acid; D014197:Trees
D000485:Allergens; D018076:DNA, Complementary; C107504:OLE6 protein, Olea europaea; D010940:Plant Proteins; D007073:Immunoglobulin E