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2.
Allergy ; 57 Suppl 72: 106-10, 2002.
Article in English | MEDLINE | ID: mdl-12144567

ABSTRACT

Plant-origin foods, especially nuts and seeds, are the most important sources of food allergic reactions. An important characteristic is the quantitative and qualitative variability of their content in allergenic molecules, depending on plant growth, ripening, environmental stresses or industrial processing. In this review we will focus on newly identified allergens. Recent research have characterized and extensively studied their biochemistry, structure and immunological properties.


Subject(s)
Allergens , Food Hypersensitivity/etiology , Plants, Edible/immunology , Edible Grain/immunology , Fabaceae/immunology , Fruit/immunology , Humans
4.
J Chromatogr B Biomed Sci Appl ; 756(1-2): 95-103, 2001 May 25.
Article in English | MEDLINE | ID: mdl-11419731

ABSTRACT

BACKGROUND: Allergy to Prunoideae fruit (plum, peach, cherry and apricot) is one of the most frequent food allergies in southern Europe. All these fruits cross-react in vivo and in vitro, as they share their major allergen, a 9 kD lipid transfer protein (LTP). OBJECTIVE: The aim of the study was the identification and molecular characterization of the major allergen of plum. METHODS: The IgE pattern of reactivity to plums was investigated by SDS-PAGE and immunoblotting with the sera of 23 patients. The identified major allergen was purified by HPLC, using a cationic-exchange column followed by gel-filtration. Further characterization was achieved by periodic-Schiff stain, isoelectrofocusing and N-terminal amino acid sequencing. RESULTS AND CONCLUSIONS: The major allergen of plum is a 9 kD lipid transfer protein, not glycosylated and with a basic character (pI>9), highly homologous to the major allergen of peach.


Subject(s)
Allergens/chemistry , Carrier Proteins/chemistry , Fruit/immunology , Adolescent , Adult , Amino Acid Sequence , Antigens, Plant , Blotting, Western , Carrier Proteins/metabolism , Chromatography, Gel , Chromatography, High Pressure Liquid , Chromatography, Ion Exchange , Cross Reactions , Electrophoresis, Polyacrylamide Gel , Female , Humans , Immunoglobulin E/metabolism , In Vitro Techniques , Male , Middle Aged , Molecular Sequence Data , Plant Proteins , Protein Binding
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