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Keywords:

  • food allergy;
  • IgE;
  • peanuts;
  • soybeans;
  • oleosin

Background : Peanut allergy is one of the five most frequent food allergies in children and in adults. Recently, we purified and evaluated the allergenicity of peanut oleosins, a family of small-sized proteins involved in the formation of peanut oil bodies.

Methods:  Allergenicity of the purified native protein and of the recombinant protein was tested by Western blot and by IgE-RIA.

Results:  We found IgE-binding with oleosin in 3 of 14 sera of patients who had suffered an allergic reaction to peanuts. Two sera reacted weakly against 16–18 kDa proteins corresponding to oleosin monomers, in Western blot. The main reacting bands had a molecular size estimated at ≈34 kDa, ≈50 kDa and ≈ 68 kDa and could therefore correspond to oleosin oligomers. IgE reactivity was higher in extracts from roasted peanuts. The same phenomenon occurred with crude soybean oil fraction, with two bands of 16.5 and 24 kDa corresponding to monomers, and two bands of 50 kDa and 76 kDa corresponding to dimers and trimers, respectively. The 18 kDa band was observed in the 3 Western blots of a membrane-enriched fraction of recombinant oleosin produced in the Sf9-baculovirus expression system (performed with the 3 patient sera).

Conclusions:  We have characterized a new peanut allergen which belongs to the oleosins, a family of proteins involved in the formation of oil bodies. The protein may be involved in some of the allergic cross-reactions to peanuts and soybeans.