Purification, amino acid sequence and immunological characterization of Ole e 6, a cysteine-enriched allergen from olive tree pollen

FEBS Lett. 1997 Jun 30;410(2-3):293-6. doi: 10.1016/s0014-5793(97)00582-6.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Allergens / chemistry
  • Allergens / genetics
  • Allergens / immunology
  • Allergens / isolation & purification*
  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Cloning, Molecular
  • DNA, Complementary
  • Humans
  • Immunoglobulin E / immunology
  • Molecular Sequence Data
  • Plant Proteins / chemistry
  • Plant Proteins / genetics
  • Plant Proteins / immunology
  • Plant Proteins / isolation & purification*
  • Pollen*
  • Rabbits
  • Sequence Homology, Amino Acid
  • Trees

Substances

  • Allergens
  • DNA, Complementary
  • OLE6 protein, Olea europaea
  • Plant Proteins
  • Immunoglobulin E

Associated data

  • GENBANK/U86342