Publication Date:
2001
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. © 2001 Elsevier Science B.V.
Iris type:
01.01 Articolo in rivista
Keywords:
Allergies; Amino acids; Filtration; Fruits; Gels; Lipids; Patient monitoring; Proteins; Food allergies; Chromatography; food allergen; immunoglobulin E antibody; lipid transfer protein; adult; amino terminal sequence; article; cation exchange; clinical article; clinical trial; controlled clinical trial; controlled study; female; food allergy; fruit; gel filtration; high performance liquid chromatography; human; immunoblotting; immunoreactivity; isoelectric focusing; male; polyacry; priority journal; protein analysis; Adolescent; Adult; Allergens; Amino Acid Sequence; Antigens; Plant; Blotting; Western; Carrier Proteins; Chromatography; Gel; Chromatography; High Pressure Liquid; Chromatography; Ion Exchange; Cross Reactions; Electrophoresis; Polyacrylamide Gel; Female; Fruit; Humans; Immunoglobulin E; Male; Middle Aged; Molecular Sequence Data; Plant Proteins; Protein Binding
List of contributors:
Conti, Amedeo; Giuffrida, MARIA GABRIELLA; Fortunato, Donatella
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