Molecular characterization of Phl p II, a major timothy grass (Phleum pratense) pollen allergen.
FEBS Lett
; 335(3): 299-304, 1993 Dec 13.
Article
in En
| MEDLINE
| ID: mdl-8262175
ABSTRACT
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.
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Database:
MEDLINE
Main subject:
Plant Proteins
/
Pollen
/
Allergens
/
Poaceae
Limits:
Humans
Language:
En
Journal:
FEBS Lett
Year:
1993
Type:
Article
Affiliation country:
Austria