Characterization of the major allergen of plum as a lipid transfer protein

J Chromatogr B Biomed Sci Appl. 2001 May 25;756(1-2):95-103. doi: 10.1016/s0378-4347(01)00074-3.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

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

Substances

  • Allergens
  • Antigens, Plant
  • Carrier Proteins
  • Plant Proteins
  • lipid transfer proteins, plant
  • Immunoglobulin E