CHARACTERIZATION OF DER-P-V-ALLERGEN, CDNA ANALYSIS, AND IGE-MEDIATED REACTIVITY 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 produced IgE-binding proteins were isolated. Their sequences were homologous to that of a cDNA described previously which contained a reading frame encoding a 17 kd polypeptide and which as determined by serologic analysis corresponded to a protein with relative molecular mass of 14 kd in mite extracts. The cDNA from the lambda gt11 clones was truncated so if was used to obtain longer clones from a lambda gt10 library. Analysis of the sequence of these clones showed that the allergen now designated Der p V is produced from a 132-residue polypeptide, which has a putative 19-residue leader peptide and a 213-residue mature protein. This would have a molecular weight of 14 kd, corresponding to that found in mite extracts. IgE binding studies with the lambda gt11 clone and a fusion of the mature sequence in a pGEX construct showed that it reacted with 50% of allergic sera. Further studies with skin tests indicated that it caused reactions in about 60% of patients with asthma and 29% of chose with allergic rhinitis alone.