Food and drug reactions and anaphylaxisThe maize major allergen, which is responsible for food-induced allergic reactions, is a lipid transfer protein☆,☆☆
Section snippets
Patients
Patients referred to the Allergy Centre of the 3rd Department of General Medicine, University of Milan, or to the Bizzozzero Division of “Niguarda Ca’ Granda” Hospital, Milan, were selected on the basis of documented food-induced allergic reactions to maize. All patients who reported systemic anaphylaxis after eating maize in different forms (eg, polenta, popcorn, or crisps) were recruited for the study. A detailed clinical history revealed that before presenting systemic symptoms, some
Patients
Twenty-two patients, 16 women and 6 men, aged from 12 to 50 years (mean age, 28.4 years) were recruited for the in vitro study. All had severe systemic reactions to maize documented by visits to hospital emergency departments. Three had exercise-induced food-dependent anaphylaxis. Nine patients reported OAS before experiencing systemic symptoms. The demographic data, maize-specific IgE values (CAP System), symptoms elicited by maize, pollens responsible for respiratory symptoms, and history of
Discussion
The major allergen of maize, which is responsible for provoking food-induced allergic reactions, was found to be an LTP. This protein was fully sequenced in 1988 and was shown to share with other LTPs the same low MW (approximately 9 kd), the basic characteristic (isoelectric point between 9 and 10), and, most importantly, the presence of conserved residues, such as 8 cysteines forming 4 disulphur bridges, in the amino acid sequence.17 Its three-dimensional structure was recently deduced from
References (27)
- et al.
Immunologic cross-reactivity among cereal grains and grasses in children with food hypersensitivity
J Allergy Clin Immunol
(1995) - et al.
Allergenic cross-reactivity between peach, apricot, plum and cherry in patients with oral allergy syndrome: an in-vivo and in-vitro study
J Allergy Clin Immunol
(1994) - et al.
Allergy to Rosaceae fruits without related pollinosis
J Allergy Clin Immunol
(1997) - et al.
The major allergen of peach (Prunus persica) is a lipid transfer protein
J Allergy Clin Immunol
(1999) - et al.
Food-dependent exercise-induced anaphylaxis to corn
J Allergy Clin Immunol
(1998) - et al.
Studies of hypersensitivity reactions to food in infants and children
J Allergy Clin Immunol
(1978) - et al.
Classification of rice allergenic protein cDNAs belonging to the α-amylase/trypsin inhibitor gene family
Biochim Biophys Acta
(1995) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
Anal Biochem
(1976)Molecular weight determination of protein-dodecyl sulfate complexes by gel electrophoresis in a discontinuous buffer system
J Biol Chem
(1971)- et al.
Immunoblotting and dot immunoblotting current status and outlook
J Immunol Methods
(1984)
Phospholipid transfer protein: full-length cDNA and amino acid sequence in maize. Aminoacid sequence homologies between plant phospholipid transfer proteins
J Biol Chem
High-resolution crystal structure of the non-specific lipid-transfer protein from maize seedling
Structure
Amino acid sequence and secondary structural analysis of the corn inhibitor of trypsin and activated Hageman factor
J Biol Chem
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Supported in part by a grant from the European Commission (No. FAIR-CT97-3224).
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Reprint requests: Elide A. Pastorello, MD, 3rd Division of General Medicine, Padiglione Granelli, Via Francesco Sforza 35, 20122 Milan, Italy.