The maize major allergen, which is responsible for food-induced allergic reactions, is a lipid transfer protein.
BACKGROUND
Cereals are the most important nutritional component in the human diet. Food-induced allergic reactions to these substances therefore have serious implications, and exhaustive diagnosis is required. Such diagnosis is still difficult because of the incomplete knowledge about major cereal allergens. In particular, few food-induced allergic reactions to maize have been reported, and no information on the allergenic proteins is available.


OBJECTIVE
Having observed several anaphylactic reactions to maize, we planned a study to identify maize major allergens and cross-reactivity with other cereals, as well as to peach because the majority of patients also reacted to Prunoideae fruits.


METHODS
Twenty-two patients with systemic symptoms after maize ingestion and positive skin prick test responses and serum-specific IgE antibodies to maize were selected. The IgE-reactivity pattern was identified by SDS-PAGE and immunoblotting. The major allergen identified was then purified by HPLC and characterized by mass spectrometry, determination of the isoelectric point value, and N-terminal amino acid sequencing.


RESULTS
Sera from 19 (86%) of the 22 patients recognized a 9-kd protein, thus confirming this as the maize major allergen. This protein had an isoelectric point of greater than 9, a molecular mass of 9047.0 d, and no glycosylation. Determination of its N-terminal sequence showed that it was a lipid transfer protein (LTP). By using immunoblotting-inhibition experiments, we demonstrated that the LTP cross-reacts completely with rice and peach LTPs but not with wheat or barley LTPs. N-terminal sequence of the 16-kd allergen (recognized by 36% of patients) showed it to be the maize inhibitor of trypsin. This protein cross-reacts completely with grass, wheat, barley, and rice trypsin inhibitors.


CONCLUSIONS
The major allergen of maize is an LTP with a molecular weight of 9 kd that is highly homologous with the peach LTP, the major allergen of the Prunoideae subfamily.
Pastorello
E A
EA
Allergy Centre, 3rd Division of General Medicine, Ospedale Maggiore IRCCS, Milan, Italy.
Farioli
L
L
Pravettoni
V
V
Ispano
M
M
Scibola
E
E
Trambaioli
C
C
Giuffrida
M G
MG
Ansaloni
R
R
Godovac-Zimmermann
J
J
Conti
A
A
Fortunato
D
D
Ortolani
C
C
D000293:Adolescent; D000328:Adult; D000485:Allergens / Q000276:immunology* / Q000302:isolation & purification; D052179:Antigens, Plant; D002352:Carrier Proteins / Q000276:immunology*; D002648:Child; D002851:Chromatography, High Pressure Liquid; D005260:Female; D005512:Food Hypersensitivity / Q000276:immunology*; D006801:Humans; D015151:Immunoblotting; D007073:Immunoglobulin E / Q000378:metabolism; D007525:Isoelectric Focusing; D008297:Male; D013058:Mass Spectrometry; D008875:Middle Aged; D010940:Plant Proteins; D011485:Protein Binding; D003313:Zea mays / Q000276:immunology*
D000485:Allergens; D052179:Antigens, Plant; D002352:Carrier Proteins; D010940:Plant Proteins; C511920:lipid transfer proteins, plant; D007073:Immunoglobulin E