Molecular characterization of Phl p II, a major timothy grass (Phleum pratense) pollen allergen

FEBS Lett. 1993 Dec 13;335(3):299-304. doi: 10.1016/0014-5793(93)80406-k.


Grass pollen allergens belong to the most important and widespread elicitors of pollen allergy. Using serum IgE from a grass pollen allergic patient, a complete cDNA encoding a group II allergen was isolated from a timothy grass (Phleum pratense) pollen expression library. The deduced amino acid sequence of the Phl p II allergen shows an average sequence identity of 61% with the protein sequences determined for group II/III allergens from rye grass (Lolium perenne) and a sequence identity of 43% with the C-terminal portion of group I grass pollen allergens from different species. A hydrophobic leader peptide similar to leader peptides found in other major grass pollen allergens heads the deduced amino acid sequence, indicating that group II/III grass pollen allergens belong to a family of secreted proteins. Serum IgE specific for Phl p II, detected the protein exclusively in pollen and not in other plant tissues. The recombinant Phl p II was expressed in Escherichia coli and showed similar IgE-binding capacity as the natural allergen.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Allergens / genetics*
  • Allergens / immunology
  • Amino Acid Sequence
  • Base Sequence
  • Cross Reactions
  • DNA
  • Humans
  • Immunoglobulin E / immunology
  • Molecular Sequence Data
  • Plant Proteins / genetics*
  • Plant Proteins / immunology
  • Poaceae / genetics*
  • Poaceae / immunology
  • Pollen / genetics*
  • Pollen / immunology
  • Sequence Homology, Amino Acid


  • Allergens
  • PHLPII protein, Phleum pratense
  • Plant Proteins
  • Immunoglobulin E
  • DNA

Associated data

  • GENBANK/X75925