A cDNA coding for the major group V allergen Phl p Vb was isolated fro
m a timothy grass pollen cDNA library by immunoscreening with a specif
ic monoclonal antibody. It was discovered for the first time that the
recombinant Phl p Vb pollen allergen after expression and purification
has ribonuclease activity. High homology of Phl p Vb to other group V
allergens in grass pollen indicates similar function. By RNase activi
ty gel of natural pollen extract of timothy grass and consecutive West
ern blot analysis of the excised proteins, the RNase active bands were
shown to be group V allergens. Additionally it was demonstrated that
an homologous protein to Phl p Vb in the mother plant could be induced
by salicylic acid. This indicates that group Vb allergens may be invo
lved in host-pathogen interactions because in pollen they are quickly
exported RNases and in the mother plant they depend on a hormone which
is related to expression of plant resistance genes.