Primary structure, recombinant expression, and molecular characterization of Phl p 4, a major allergen of timothy grass (Phleum pratense)

Biochem Biophys Res Commun. 2005 Nov 18;337(2):563-70. doi: 10.1016/j.bbrc.2005.09.087. Epub 2005 Sep 22.

Abstract

Grass pollen allergy is one of the most important allergic diseases world-wide. Several meadow grasses, like timothy grass and rye grass, contribute to allergic sensitizations, but also allergens from extensively cultivated cereals, especially rye, make a profound contribution. The group 4 allergens are well known as important major allergens of grasses. We have cloned for the first time group 4 sequences from Phleum pratense, Lolium perenne, Secale cereale, Triticum aestivum, and Hordeum vulgare, and investigated the IgE-reactivity of recombinant Phl p 4 as a candidate for allergy diagnostic and therapeutic applications.

MeSH terms

  • Allergens / chemistry
  • Allergens / genetics
  • Allergens / metabolism*
  • Amino Acid Sequence
  • Base Sequence
  • Cloning, Molecular
  • Gene Expression
  • Molecular Sequence Data
  • Phleum / chemistry*
  • Plant Proteins / chemistry
  • Plant Proteins / genetics
  • Plant Proteins / metabolism*
  • Recombinant Proteins / genetics
  • Recombinant Proteins / immunology
  • Recombinant Proteins / metabolism

Substances

  • Allergens
  • Phl p 4 protein, Phleum pratense
  • Plant Proteins
  • Recombinant Proteins

Associated data

  • GENBANK/AJ512487
  • GENBANK/AJ512488
  • GENBANK/AJ862830
  • GENBANK/AJ862831
  • GENBANK/AJ862832
  • GENBANK/AJ862833
  • GENBANK/AJ862834
  • GENBANK/AJ862835