molecular cloning and expression of pro j 1: a new allergen of prosopis juliflora pollen

pollen from mesquite (prosopis juliflora) is one of the important causes of immediate hypersensitivity reactions in the arid and semi-arid regions of the world. the aim of present study is to produce and purify the recombinant form of allergenic ole e 1-like protein from the pollen of this allergenic tree. immunological and cross-inhibition assays were performed for the evaluation of ige-binding capacity of purified recombinant protein. for molecular cloning, the coding sequence of the mesquite ole e 1-like protein was inserted into ptz57r/t vector and expressed in escherichia coli using the vector pet-21b(+). after purification of the recombinant protein, its immunoreactivity was analysed by in vitro assays using sera from twenty one patients with an allergy to mesquite pollen. the purified recombinant allergen was a member of ole e 1-like protein family and consisted of 150 amino acid residues, with a predicted molecular mass of 16.5 kda and a calculated isoelectric point (pi) of 4.75. twelve patients (57.14%) had significant specific ige levels for this recombinant allergen. immunodetection and inhibition assays indicated that the purified recombinant allergen might be the same as that in the crude extract. herein, we introduce an important new allergen from p. juliflora pollen (pro j 1), which is a member of the ole e 1-like protein family and exhibits significant identity and similarity to other allergenic members of this family.