Strong allergenicity of Pru av 3, the lipid transfer protein from cherry, is related to high stability against thermal processing and digestion.
BACKGROUND
Nonspecific lipid transfer proteins (nsLTPs) have been identified as major fruit allergens in patients from the Mediterranean area. Sensitization to nsLTPs is accompanied by severe reactions, possibly because of specific biophysical and biochemical properties of this allergen family.


OBJECTIVE
To assess the protein stability and allergenic potency of nsLTP from fruits in comparison with birch pollen-related allergens from the same allergenic source.


METHODS
Stability of natural and recombinant cherry allergens Pru av 3 (nsLTP), Pru av 1 (Bet v 1 homologue), and Pru av 4 (profilin) to pepsin digestion and to thermal processing and stability of allergens in skin prick test reagents was investigated by immunoblotting and/or circular dichroism spectroscopy. Moreover, allergenicity of processed and fresh fruits in regard to Pru av 1 and Pru av 3 was analyzed by histamine release assays.


RESULTS
Lipid transfer proteins showed the highest resistance to digestion by pepsin (rPru av 3 > rPru av 1 > rPru av 4). Immunologically active Pru av 3 was detectable after 2 hours of digestion by pepsin, whereas IgE reactivity of Pru av 1 and Pru av 4 was abolished within less than 60 minutes. In contrast with Pru av 1, IgE reactivity to nsLTPs was not diminished in thermally processed fruits, and secondary structures of purified Pru av 3 were more resistant to heating. Moreover, nsLTPs were stable components in skin prick test reagents. Histamine release assays confirmed the strong allergenicity of nsLTPs, which was not affected by protease treatment or thermal processing of fruits.


CONCLUSIONS
In contrast with birch pollen-related allergens, nsLTPs are highly stable to pepsin treatment and thermal processing and show higher allergenic potency. Therefore, nsLTPs have the potential to act as true food allergens, probably eliciting severe systemic reactions by reaching the intestinal mucosa in an intact and fully active form.
Department of Allergology, Paul-Ehrlich-Institut, Langen, Germany. Schst@pei.de
Stephan
S
Scheurer
Iris
I
Lauer
Kay
K
Foetisch
Mar
M
San Miguel Moncin
Mechthild
M
Retzek
Christina
C
Hartz
Ernesto
E
Enrique
Jonas
J
Lidholm
Anna
A
Cistero-Bahima
Stefan
S
Vieths
D000485:Allergens / Q000276:immunology*; D052179:Antigens, Plant; D029662:Betula / Q000276:immunology; D002352:Carrier Proteins / Q000378:metabolism*; D004063:Digestion / Q000502:physiology; D005512:Food Hypersensitivity / Q000276:immunology*; D006358:Hot Temperature; D006801:Humans; D006967:Hypersensitivity / Q000276:immunology; D010940:Plant Proteins; D011058:Pollen / Q000276:immunology; D027861:Prunus / Q000276:immunology*
D000485:Allergens; D052179:Antigens, Plant; D002352:Carrier Proteins; D010940:Plant Proteins; C511920:lipid transfer proteins, plant