Kl. Lin et al., CHARACTERIZATION OF DER-P-V-ALLERGEN, CDNA ANALYSIS, AND IGE-MEDIATEDREACTIVITY TO THE RECOMBINANT PROTEIN, Journal of allergy and clinical immunology, 94(6), 1994, pp. 989-996
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.