The major allergen of peach (Prunus persica) is a lipid transfer protein

Elide A. Pastorello, Laura Farioli, Valerio Pravettoni, Claudio Ortolani, Marco Ispano, Mara Monza, Chiara Baroglio, Elisabetta Scibola, Raffaella Ansaloni, Cristoforo Incorvaia, Amedeo Conti

Research output: Contribution to journalArticle

245 Citations (Scopus)

Abstract

Background: Allergy to fresh fruits and vegetables is mostly observed in subjects with pollinosis, especially from birch, because of cross-reacting allergens in vegetable foods and pollens. However, allergic reactions to fruits, specifically Rosaceae fruits, have been reported in subjects without pollinosis. Objective: This study evaluated the pattern of IgE reactivity, identifying the allergen responsible in 2 groups of patients with oral allergy syndrome to peach with or without birch pollinosis. Methods: The allergenic components of peach were detected by SDS-PAGE and immunoblotting. The major peach allergen was purified by HPLC with a cation-exchange column followed by gel filtration chromatography. Its IgE-binding capacity and its homology with the protein of the crude extract were demonstrated by immunoblotting inhibition techniques. To better characterize this allergen, periodic acid-Schiff stain and isoelectrofocusing were used. The amino acid sequencing was done with a gas-phase sequencer. Results: SDS-PAGE and immunoblotting of the 15 patients allergic to peach, 8 without and 7 with birch pollinosis, showed that they all recognized a protein with a molecular weight of 9 kd. This was the only allergen recognized by patients not sensitized to pollen, whereas the birch pollen-sensitive patients had IgE binding to other allergenic proteins at higher molecular weights. The purified 9-kd protein retained its IgE-binding capacity, was negative to periodic acid-Schiff stain, and had an isoelectric point value of greater than 9. A search in the Swiss Prot Bank showed this was a lipid transfer protein, belonging to a group of molecules involved in the defensive system of plants. Conclusions: The major allergen of peach is a 9-kd protein belonging to the group of lipid transfer proteins. This is the only allergen recognized by patients allergic to peach but not sensitized to birch pollen.

Original languageEnglish
Pages (from-to)520-526
Number of pages7
JournalJournal of Allergy and Clinical Immunology
Volume103
Issue number3 II
Publication statusPublished - 1999

Fingerprint

Allergens
Betula
Seasonal Allergic Rhinitis
Pollen
Immunoglobulin E
Immunoblotting
Fruit
Hypersensitivity
Periodic Acid
Proteins
Vegetables
Polyacrylamide Gel Electrophoresis
Coloring Agents
Molecular Weight
Rosaceae
Protein Sequence Analysis
Isoelectric Point
Prunus persica
lipid transfer protein
Complex Mixtures

Keywords

  • Birch pollinosis
  • Immunoblotting
  • Lipid transfer protein
  • Major allergen
  • Oral allergy syndrome
  • Peach

ASJC Scopus subject areas

  • Immunology
  • Immunology and Allergy

Cite this

Pastorello, E. A., Farioli, L., Pravettoni, V., Ortolani, C., Ispano, M., Monza, M., ... Conti, A. (1999). The major allergen of peach (Prunus persica) is a lipid transfer protein. Journal of Allergy and Clinical Immunology, 103(3 II), 520-526.

The major allergen of peach (Prunus persica) is a lipid transfer protein. / Pastorello, Elide A.; Farioli, Laura; Pravettoni, Valerio; Ortolani, Claudio; Ispano, Marco; Monza, Mara; Baroglio, Chiara; Scibola, Elisabetta; Ansaloni, Raffaella; Incorvaia, Cristoforo; Conti, Amedeo.

In: Journal of Allergy and Clinical Immunology, Vol. 103, No. 3 II, 1999, p. 520-526.

Research output: Contribution to journalArticle

Pastorello, EA, Farioli, L, Pravettoni, V, Ortolani, C, Ispano, M, Monza, M, Baroglio, C, Scibola, E, Ansaloni, R, Incorvaia, C & Conti, A 1999, 'The major allergen of peach (Prunus persica) is a lipid transfer protein', Journal of Allergy and Clinical Immunology, vol. 103, no. 3 II, pp. 520-526.
Pastorello EA, Farioli L, Pravettoni V, Ortolani C, Ispano M, Monza M et al. The major allergen of peach (Prunus persica) is a lipid transfer protein. Journal of Allergy and Clinical Immunology. 1999;103(3 II):520-526.
Pastorello, Elide A. ; Farioli, Laura ; Pravettoni, Valerio ; Ortolani, Claudio ; Ispano, Marco ; Monza, Mara ; Baroglio, Chiara ; Scibola, Elisabetta ; Ansaloni, Raffaella ; Incorvaia, Cristoforo ; Conti, Amedeo. / The major allergen of peach (Prunus persica) is a lipid transfer protein. In: Journal of Allergy and Clinical Immunology. 1999 ; Vol. 103, No. 3 II. pp. 520-526.
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abstract = "Background: Allergy to fresh fruits and vegetables is mostly observed in subjects with pollinosis, especially from birch, because of cross-reacting allergens in vegetable foods and pollens. However, allergic reactions to fruits, specifically Rosaceae fruits, have been reported in subjects without pollinosis. Objective: This study evaluated the pattern of IgE reactivity, identifying the allergen responsible in 2 groups of patients with oral allergy syndrome to peach with or without birch pollinosis. Methods: The allergenic components of peach were detected by SDS-PAGE and immunoblotting. The major peach allergen was purified by HPLC with a cation-exchange column followed by gel filtration chromatography. Its IgE-binding capacity and its homology with the protein of the crude extract were demonstrated by immunoblotting inhibition techniques. To better characterize this allergen, periodic acid-Schiff stain and isoelectrofocusing were used. The amino acid sequencing was done with a gas-phase sequencer. Results: SDS-PAGE and immunoblotting of the 15 patients allergic to peach, 8 without and 7 with birch pollinosis, showed that they all recognized a protein with a molecular weight of 9 kd. This was the only allergen recognized by patients not sensitized to pollen, whereas the birch pollen-sensitive patients had IgE binding to other allergenic proteins at higher molecular weights. The purified 9-kd protein retained its IgE-binding capacity, was negative to periodic acid-Schiff stain, and had an isoelectric point value of greater than 9. A search in the Swiss Prot Bank showed this was a lipid transfer protein, belonging to a group of molecules involved in the defensive system of plants. Conclusions: The major allergen of peach is a 9-kd protein belonging to the group of lipid transfer proteins. This is the only allergen recognized by patients allergic to peach but not sensitized to birch pollen.",
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T1 - The major allergen of peach (Prunus persica) is a lipid transfer protein

AU - Pastorello, Elide A.

AU - Farioli, Laura

AU - Pravettoni, Valerio

AU - Ortolani, Claudio

AU - Ispano, Marco

AU - Monza, Mara

AU - Baroglio, Chiara

AU - Scibola, Elisabetta

AU - Ansaloni, Raffaella

AU - Incorvaia, Cristoforo

AU - Conti, Amedeo

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Y1 - 1999

N2 - Background: Allergy to fresh fruits and vegetables is mostly observed in subjects with pollinosis, especially from birch, because of cross-reacting allergens in vegetable foods and pollens. However, allergic reactions to fruits, specifically Rosaceae fruits, have been reported in subjects without pollinosis. Objective: This study evaluated the pattern of IgE reactivity, identifying the allergen responsible in 2 groups of patients with oral allergy syndrome to peach with or without birch pollinosis. Methods: The allergenic components of peach were detected by SDS-PAGE and immunoblotting. The major peach allergen was purified by HPLC with a cation-exchange column followed by gel filtration chromatography. Its IgE-binding capacity and its homology with the protein of the crude extract were demonstrated by immunoblotting inhibition techniques. To better characterize this allergen, periodic acid-Schiff stain and isoelectrofocusing were used. The amino acid sequencing was done with a gas-phase sequencer. Results: SDS-PAGE and immunoblotting of the 15 patients allergic to peach, 8 without and 7 with birch pollinosis, showed that they all recognized a protein with a molecular weight of 9 kd. This was the only allergen recognized by patients not sensitized to pollen, whereas the birch pollen-sensitive patients had IgE binding to other allergenic proteins at higher molecular weights. The purified 9-kd protein retained its IgE-binding capacity, was negative to periodic acid-Schiff stain, and had an isoelectric point value of greater than 9. A search in the Swiss Prot Bank showed this was a lipid transfer protein, belonging to a group of molecules involved in the defensive system of plants. Conclusions: The major allergen of peach is a 9-kd protein belonging to the group of lipid transfer proteins. This is the only allergen recognized by patients allergic to peach but not sensitized to birch pollen.

AB - Background: Allergy to fresh fruits and vegetables is mostly observed in subjects with pollinosis, especially from birch, because of cross-reacting allergens in vegetable foods and pollens. However, allergic reactions to fruits, specifically Rosaceae fruits, have been reported in subjects without pollinosis. Objective: This study evaluated the pattern of IgE reactivity, identifying the allergen responsible in 2 groups of patients with oral allergy syndrome to peach with or without birch pollinosis. Methods: The allergenic components of peach were detected by SDS-PAGE and immunoblotting. The major peach allergen was purified by HPLC with a cation-exchange column followed by gel filtration chromatography. Its IgE-binding capacity and its homology with the protein of the crude extract were demonstrated by immunoblotting inhibition techniques. To better characterize this allergen, periodic acid-Schiff stain and isoelectrofocusing were used. The amino acid sequencing was done with a gas-phase sequencer. Results: SDS-PAGE and immunoblotting of the 15 patients allergic to peach, 8 without and 7 with birch pollinosis, showed that they all recognized a protein with a molecular weight of 9 kd. This was the only allergen recognized by patients not sensitized to pollen, whereas the birch pollen-sensitive patients had IgE binding to other allergenic proteins at higher molecular weights. The purified 9-kd protein retained its IgE-binding capacity, was negative to periodic acid-Schiff stain, and had an isoelectric point value of greater than 9. A search in the Swiss Prot Bank showed this was a lipid transfer protein, belonging to a group of molecules involved in the defensive system of plants. Conclusions: The major allergen of peach is a 9-kd protein belonging to the group of lipid transfer proteins. This is the only allergen recognized by patients allergic to peach but not sensitized to birch pollen.

KW - Birch pollinosis

KW - Immunoblotting

KW - Lipid transfer protein

KW - Major allergen

KW - Oral allergy syndrome

KW - Peach

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