CHARACTERIZATION OF DER-P-V-ALLERGEN, CDNA ANALYSIS, AND IGE-MEDIATEDREACTIVITY TO THE RECOMBINANT PROTEIN

A lambda gt11 library for cDNA from Dermatophagoides pteronyssinus was screened by plaque immunoassay, and a number of related clones that p roduced IgE-binding proteins were isolated. Their sequences were homol ogous to that of a cDNA described previously which contained a reading frame encoding a 17 kd polypeptide and which as determined by serolog ic analysis corresponded to a protein with relative molecular mass of 14 kd in mite extracts. The cDNA from the lambda gt11 clones was trunc ated so if was used to obtain longer clones from a lambda gt10 library . Analysis of the sequence of these clones showed that the allergen no w designated Der p V is produced from a 132-residue polypeptide, which has a putative 19-residue leader peptide and a 213-residue mature pro tein. This would have a molecular weight of 14 kd, corresponding to th at found in mite extracts. IgE binding studies with the lambda gt11 cl one and a fusion of the mature sequence in a pGEX construct showed tha t it reacted with 50% of allergic sera. Further studies with skin test s indicated that it caused reactions in about 60% of patients with ast hma and 29% of chose with allergic rhinitis alone.