Structural investigations of the major allergen Phl p I on the complementary DNA and protein level, ,
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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 l 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. (J ALLERGY CLIN IMMUNOL 1995;95:987-94.)
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