TY - JOUR
T1 - Wheat IgE-mediated food allergy in european patients
T2 - α-amylase inhibitors, lipid transfer proteins and low-molecular-weight glutenins - Allergenic molecules recognized by double-blind, placebo-controlled food challenge
AU - Pastorello, Elide A.
AU - Farioli, Laura
AU - Conti, Amedeo
AU - Pravettoni, Valerio
AU - Bonomi, Simona
AU - Iametti, Stefania
AU - Fortunato, Donatella
AU - Scibilia, Joseph
AU - Bindslev-Jensen, Carsten
AU - Ballmer-Weber, Barbara
AU - Robino, Anna M.
AU - Ortolani, Claudio
PY - 2007/8
Y1 - 2007/8
N2 - Background: Three main problems hamper the identification of wheat food allergens: (1) lack of a standardized procedure for extracting all of the wheat protein fractions; (2) absence of double-blind, placebo-controlled food challenge studies that compare the allergenic profile of Osborne's three protein fractions in subjects with real wheat allergy, and (3) lack of data on the differences in IgE-binding capacity between raw and cooked wheat. Methods: Sera of 16 wheat-challenge-positive patients and 6 patients with wheat anaphylaxis, recruited from Italy, Denmark and Switzerland, were used for sodium dodecyl sulfate-polyacrylamide gel electrophoresis/immunoblotting of the three Osborne's protein fractions (albumin/globulin, gliadins and glutenins) of raw and cooked wheat. Thermal sensitivity of wheat lipid transfer protein (LTP) was investigated by spectroscopic approaches. IgE cross-reactivity between wheat and grass pollen was studied by blot inhibition. Results: The most important wheat allergens were the α-amylase/trypsin inhibitor subunits, which were present in all three protein fractions of raw and cooked wheat. Other important allergens were a 9-kDa LTP in the albumin/globulin fraction and several low-molecular-weight (LMW) glutenin subunits in the gluten fraction. All these allergens showed heat resistance and lack of cross-reactivity to grass pollen allergens. LTP was a major allergen only in Italian patients. Conclusions: The α-amylase inhibitor was confirmed to be the most important wheat allergen in food allergy and to play a role in wheat-dependent exercise-induced anaphylaxis, too. Other important allergens were LTP and the LMW glutenin subunits.
AB - Background: Three main problems hamper the identification of wheat food allergens: (1) lack of a standardized procedure for extracting all of the wheat protein fractions; (2) absence of double-blind, placebo-controlled food challenge studies that compare the allergenic profile of Osborne's three protein fractions in subjects with real wheat allergy, and (3) lack of data on the differences in IgE-binding capacity between raw and cooked wheat. Methods: Sera of 16 wheat-challenge-positive patients and 6 patients with wheat anaphylaxis, recruited from Italy, Denmark and Switzerland, were used for sodium dodecyl sulfate-polyacrylamide gel electrophoresis/immunoblotting of the three Osborne's protein fractions (albumin/globulin, gliadins and glutenins) of raw and cooked wheat. Thermal sensitivity of wheat lipid transfer protein (LTP) was investigated by spectroscopic approaches. IgE cross-reactivity between wheat and grass pollen was studied by blot inhibition. Results: The most important wheat allergens were the α-amylase/trypsin inhibitor subunits, which were present in all three protein fractions of raw and cooked wheat. Other important allergens were a 9-kDa LTP in the albumin/globulin fraction and several low-molecular-weight (LMW) glutenin subunits in the gluten fraction. All these allergens showed heat resistance and lack of cross-reactivity to grass pollen allergens. LTP was a major allergen only in Italian patients. Conclusions: The α-amylase inhibitor was confirmed to be the most important wheat allergen in food allergy and to play a role in wheat-dependent exercise-induced anaphylaxis, too. Other important allergens were LTP and the LMW glutenin subunits.
KW - α-Amylase inhibitor
KW - Anaphylaxis
KW - Double-blind, placebo-controlled food challenge
KW - Food allergens
KW - Gliadins
KW - Gluten
KW - Glutenins
KW - Lipid transfer protein
KW - Thermal treatment
KW - Wheat allergy
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U2 - 10.1159/000102609
DO - 10.1159/000102609
M3 - Article
C2 - 17496422
AN - SCOPUS:34547755941
VL - 144
SP - 10
EP - 22
JO - International Archives of Allergy and Immunology
JF - International Archives of Allergy and Immunology
SN - 1018-2438
IS - 1
ER -