Cloning of a cDNA from Cryj II, the second major allergen from Japanes
e cedar (Cryptomeria japonica) pollen, is described. An isolated Cryj
II cDNA contained an open reading frame coding for 514 amino acid resi
dues. The mature Cryj II protein consisted of 388 amino acid residues
(R(46)S(433)). According to a homology analysis, no amino acid sequenc
e homology was observed between Cryj II and Cryj I, another major alle
rgen. But Cryj II showed homology with polygalacturonase (PG) derived
from tomato (40% identity) at the amino acid level. The sequence infor
mation can potentially be used to devise an effective course of immuno
therapy for Japanese cedar pollinosis.