Structural investigations of the major allergen Phl p I on the complementary DNA and protein level

J Allergy Clin Immunol. 1995 May;95(5 Pt 1):987-94. doi: 10.1016/s0091-6749(95)70099-4.

Abstract

Until now investigations of group I grass allergens have mainly been performed on ryegrass allergen (Lol p I). We studied this major allergen grass group with timothy grass pollen (Phl p I), a very common and important cause of type I allergy, to determine intraspecific and interspecific variations among different grass species. By immunoscreening a timothy grass pollen complementary DNA library we obtained three full-length clones. They revealed identical nucleotide sequences in the coding regions consisting of 262 amino acids, including a leader sequence of 23 amino acid residues. The comparison of our data with the amino acid sequences deduced from Lol p I and Hol 1 I clones showed sequence identities of greater than 85% and homologies of greater than 90%, indicating a high degree of sequence conservation. Despite the high degree of homology, amino acid differences were in immunodominant positions, which may be responsible for the differing immune response to group I allergens of different grass species.

Publication types

  • Comparative Study

MeSH terms

  • Allergens / genetics*
  • Amino Acid Sequence
  • Base Sequence
  • Cloning, Molecular
  • DNA, Complementary / genetics
  • Molecular Sequence Data
  • Plant Proteins / genetics*
  • Poaceae / genetics*
  • Poaceae / immunology
  • Pollen / genetics*
  • Pollen / immunology
  • Protein Processing, Post-Translational
  • Sequence Analysis, DNA
  • Sequence Homology, Amino Acid
  • Species Specificity

Substances

  • Allergens
  • DNA, Complementary
  • Plant Proteins
  • PHLPI protein, Phleum pratense

Associated data

  • GENBANK/Z27090