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Ann Allergy Asthma Immunol ; 99(1): 42-7, 2007 Jul.
Article in English | MEDLINE | ID: mdl-17650828

ABSTRACT

BACKGROUND: The lipid transfer protein Pru p 3 has been identified as a major peach fruit allergen. However, the putative peach member of the Bet v 1 family, Pru p 1, has been neither identified nor characterized. OBJECTIVES: To determine the distribution and solubility properties of the main peach allergens and to quantify Pru p 3 and Pru p 1 levels in peach and nectarine cultivars. METHODS: Peach peel and pulp were extracted using different buffers, and extracts were analyzed by means of sodium dodecyl sulfate-polyacrylamide gel electrophoresis and immunodetection using polyclonal antibodies against lipid transfer proteins, profilins, and Bet v 1 homologues. Pru p 3 was quantified in peach and nectarine cultivars using a sandwich enzyme-linked immunosorbent assay method. A similar method was developed to quantify Pru p 1. RESULTS: A differential distribution between peel and pulp and different solubility properties were found for Pru p 3, Pru p 1, and peach profilin. Mean Pru p 3 levels were 132.86, 0.61, and 16.92 microg/g of fresh weight of peels, pulps, and whole fruits, respectively. The corresponding mean Pru p 1 levels were 0.62, 0.26, and 0.09 microg/g of fresh weight. Most US cultivars showed higher levels of both allergens than Spanish cultivars. CONCLUSIONS: The different distribution and solubility properties of the main peach allergens can determine the quality of fruit extracts used as diagnostic tools. These differences, together with the natural variation of Pru p 3 and Pru p 1 levels among peach and nectarine cultivars, can be exploited to reduce peach allergenicity by means of industrial processing and plant breeding.


Subject(s)
Allergens/analysis , Fruit/chemistry , Prunus/chemistry , Allergens/immunology , Allergens/isolation & purification , Antigens, Plant , Blotting, Western , Enzyme-Linked Immunosorbent Assay/methods , Fruit/immunology , Plant Proteins , Prunus/classification
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