H. Breiteneder et al., Cloning of the patatin-like latex allergen Hev b 7, its expression in the yeast Pichia pastoris and its immunological characterization, INT A AL IM, 118(2-4), 1999, pp. 309-310
The 43-kD latex allergen Hev b 7 was purified from the latex of Hevea brasi
liensis and identified by N-terminal and internal peptide sequences as high
ly homologous to patatins. Patatins are storage proteins encoded by a multi
gene family found in plants such as potato and tomato, We have obtained a c
DNA clone coding for a cytoplasmic form of Hev b 7, The recombinant protein
was expressed in the methylotrophic yeast Pichia pastoris at 10 mg/l cultu
re supernatant. Both natural Hev b 7 and rHev b 7 were recognized by IgE in
11% of the latex-allergic patients, rHev b 7 inhibited binding to its coun
terpart in natural rubber latex extracts, Purified rHev b 7 used at concent
rations of in mu g/ml in skin prick tests produced wheal-and-flare reaction
s of sizes equal to those produced by nHev b 7, Furthermore, we were able t
o show that rHev b 7 possessed esterase activity. A plant expression system
for the production of larger quantities of recombinant latex allergens as
an alternative to the preparation from H. brasiliensis sap is discussed.