Allergy information for: Apricot (Prunus armeniaca )

  • Name: Apricot
  • Scientific Name: Prunus armeniaca
  • Occurrence: Apricot is consumed as fresh and processed fruit, juices, jams, jellies, preserves.
  • Allergy Information:

    Like many other allergies to fresh fruits and vegetables, apricot allergy can take two different forms. In the North of Europe, a milder form of apricot allergy is associated to birch-pollen allergy due to the similarity between a protein in birch that causes birch-pollen allergy, and an apricot protein. This is called the birch-fruit syndrome with symptoms confined largely to the mouth, causing a condition called “oral allergy syndrome” (OAS). The molecule, known as an allergen, involved in this kind of allergy does not survive cooking. Therefore, people who react to this allergen can tolerate cooked apricot. Individuals with apricot allergy might develop adverse reactions to other fruits including apple, pear, cherry, nuts such as hazelnut, or vegetables such as celeriac (celery tuber) and carrot.

    In Mediterranean countries, people with apricot allergy do not have birch-pollen allergy. Instead they often have allergy to peach. These individuals develop adverse reactions to apricot because of the similarity between the allergens in peach and apricot. Symptoms are more severe including generalised urticaria, abdominal pain, vomiting and life-threatening symptoms, sometimes in addition to the OAS. The allergen that causes this kind of allergy is tough and the allergenicity survives in processed foods such as juices and jams. As a result, individuals with this kind of allergy cannot eat even cooked fruits. Individuals with apricot allergy also tend to develop adverse reactions to other fruits including peach, apple, cherry, plum, and nuts (such as hazelnut and walnut).
  • Other Information:
  • Taxonomic Information:

    NEWT http://www.ebi.ac.uk/newt/display?from=ca&search=36596
  • Last modified: 18 October 2006

Reviews (0)

    References (0)

      Clinical History

      • Number of Studies:1-5
      • Number of Patients:>50
      • Symptoms:

        Oropharyngeal sympotoms characteristic of the oral allergy syndrome (OAS) (Pastorello et al. 1994) [156], (Pastorello et al. 2001) [152] and systematic symptoms (Pastorello et al. 2000) [150]

        In addition, Rodriguez et al. (2000) [491] described generalised anaphylaxis

      Skin Prick Test

      • Number of Studies:1-5
      • Food/Type of allergen:

        Fresh fruit and commercial apricot extracts (Pastorello et al. 1994) [156]

        Fresh fruit (Rodriguez et al. 2000) [491] (Pastorello et al. 2000) [150]

      • Protocol: (controls, definition of positive etc)

        Pastorello et al. (1994) [156] and Pastorello et al. (2000) [150] used histamine dihydrochloride (10 mg/mL) as a positive control, and the glycerol-containing diluent of the prick solution as a negative control. A wheal graded at least 2+was regarded as positive.

        Skin prick tests (SPTs) were carried out by the prick-prick technique. Histamine (10 mg/mL) and saline solution were used as positive and negative controls repectively. A positive SPT result was defined as a mean (average of orthogonal to largest diameter) wheal of 3 mm or greater (after subtracting the diameter of the wheal induced by the diluent control). (Rodriguez et al. 2000) [491]

      • Number of Patients:

        21 patients (Pastorello et al. 1994) [156]

        28 patients (Rodriguez et al. 2000) [491]

        30 patients (Pastorello et al. 2000) [150]

      • Summary of Results:

        All patients of Pastorello et al. (1994) [156] and Pastorello et al. (2000) [150] showed a positive SPT.

        SPTs were positive in 14 patients (Rodriguez et al. 2000) [491]

      IgE assay (by RAST, CAP etc)

      • Number of Studies:0
      • Food/Type of allergen:

        Commercial extracts (Rodriguez et al. 2000) [491], (Pastorello et al. 2000) [150]

      • IgE protocol:CAP (Rodriguez et al. 2000) [491], (Pastorello et al. 2000) [150]
      • Number of Patients:

        28 patients (Rodriguez et al. 2000) [491]

        30 patients (Pastorello et al. 2000) [150]

      • Summary of Results:

        18 of 28 patients had specific IgE to apricot (Rodriguez et al. 2000) [491]

        All patients had specific IgE to apricot (Pastorello et al. 2000) [150]

      Immunoblotting

      • Immunoblotting separation:

        The extracts were separated in a discontinuous buffer system in an SDS-polyacrylamide gradient gel with a 6% stacking gel and a 7.5% to 20% separation gradient. Samples were boiled and reduced with beta-mercaptoethanol (Pastorello et al. 1994) [156], (Pastorello et al. 2000) [150]

      • Immunoblotting detection method:

        The proteins were electroblotted to a nitrocellulose membrane, pore size 0.2 to 0.45 µm using a Trans-Blot Cell. The membrane was blocked with phosphate-buffered saline pH 7.4 with 0.5% (v/v) Tween 20 and incubated with the sera (diluted 1:4). The IgE-binding components were detected with iodine 125–labeled anti-human IgE antiserum diluted 1:4 (Pastorello et el. 1994) [156], (Pastorello et al. 2000) [150]

      • Immunoblotting results:

        87.5% of sera (14 of 16) of Pastorello et al. 1994 [156], showed Ig E binding to a 13 kDa protein and 77% (14 of 18) to a 30 kDa protein . The other IgE -binding components were: 70 kDa (6 of 16, 37.5%), 20 kDa (5 of 16, 31%), 14 kDa (4 of 16, 25%), 40 kDa (4 of 16, 25%) and 30 kDa (2 of 16, 12.5%). Only the component at 13 kDa was detectable in patients with negative responses to birch pollen.

        IgE immunoblotting in sera from the 30 patients showed IgE binding to proteins with molecular weights of 9 kDa (30 patients, 100%), 15 kDa (4 patients, 13.3%), 19 kDa (12 patients, 40%), 30 kDa (3 patients, 10%), 43 kDa (6 patients, 20%), 67 kDa (7 patients, 23.3%), and 80 kDa (4 patients, 13.3%) (Pastorello et al. 2000) [150]

      Oral provocation

      • Number of Studies:1-5
      • Food used and oral provocation vehicle:

        Apricot fruit (Pastorello et al. 1994) [156], (Pastorello et al. 2000) [150]

        A total of 17 g of dehydrated whole fruit was masked in a mix of orange (200 mL) and pineapple (200 mL) juices, sugar (16 g), wheat meal (13 g), and liquid coloring (Rodriguez et al. 2000) [491]

      • Blind:No. (Pastorello et al. 1994) [156], (Pastorello et al. 2000) [150]

        Open and DBPCFC (Rodriguez et al. 2000) [491]

      • Number of Patients:

        21 patients (Pastorello et al. 1994) [156]

        28 patients with positive skin prick tests or CAP System FEIA to Rosaceae (Rodriguez et al. 2000) [491]

        30 patients (Pastorello et al. 2000) [150]

      • Dose response:Patients chewed the fruit for 1 minute and then spat it out. If no symptoms appeared within 15 minutes, the challenge was repeated with increasing amounts from 4 mg up to 64 g. Patients were asked not to spit out the last two doses but to swallow the fruit instead. (Pastorello et al. 1994) [156], (Pastorello et al. 2000) [150]
      • Symptoms:

        Oropharyngeal sympotoms (itching or tingling of the lips or oral mucosa) in 6 patients (Pastorello et al. 1994) [156]

        3 patient had oropharyngeal sympotoms and two generalised anaphylaxis (Rodriguez et al. 2000) [491]

        All patients reported OAS, and 2 reported systemic symptoms to apricot (Pastorello et al. 2000) [150]

      IgE cross-reactivity and Polysensitisation

      Clinically relevant cross-reactivity between apricot and peach has been observed by immunoblot inhibition (Pastorello et al. 1994) [156].

      Other Clinical information

      Reviews (0)

        References (4)

        • Pastorello EA, D'Ambrosio FP, Pravettoni V, Farioli L, Giuffrida G, Monza M, Ansaloni R, Fortunato D, Scibola E, Rivolta F, Incorvaia C, Bengtsson A, Conti A, Ortolani C
          Evidence for a lipid transfer protein as the major allergen of apricot.
          J Allergy Clin Immunol 105:371-377. 2000
          PUBMEDID: 10669861
        • Rodriguez J; Crespo JF; Lopez-Rubio A; de la Cruz-Bertolo J; Ferrando-Vivas P; Vives R; Daroca P
          Clinical cross-reactivity among foods of the Rosaceae family.
          J Allergy Clin Immunol 106:183-189. 2000
          PUBMEDID: 10887323
        • Pastorello EA, Farioli L, Pravettoni V, Giuffrida MG, Ortolani C, Fortunato D, Trambaioli C, Scibola E, Calamari AM, Robino AM, Conti A.
          Characterization of the major allergen of plum as a lipid transfer protein.
          J Chromatogr B Biomed Sci Appl 756(1-2):95-103. 2001
          PUBMEDID: 11419731
        • Pastorello EA, Ortolani C, Farioli L, Pravettoni V, Ispano M, Borga A, Bengtsson A, Incorvaia C, Berti C, Zanussi C.
          Allergenic cross-reactivity among peach, apricot, plum, and cherry in patients with oral allergy syndrome: an in vivo and in vitro study.
          J Allergy Clin Immunol 94(4):699-707. 1994
          PUBMEDID: 7930303

        Biochemical Information for Pru ar 1

        • Allergen Name:Pru ar 1
        • Alternatve Allergen Names:
        • Allergen Designation:Major
        • Protein Family:Pathogenesis-related protein Bet v I family Pfam PF00407
        • Sequence Known?:Yes
        • Allergen accession No.s:

          O50001:Swissprot: http://ca.expasy.org/cgi-bin/niceprot.pl?O50001

          U93165; AAB97141.1; EMBL / GenBank

        • 3D Structure Accession No.:Not determined
        • Calculated Masses:17351 Da
        • Experimental Masses:17 kDa
        • Oligomeric Masses:None
        • Allergen epitopes:Not known
        • Allergen stability:
          Process, chemical, enzymatic:          Not known
        • Nature of main cross-reacting proteins:As a consequence of the homologies found between PR10 proteins in birch (Bet v 1), apple (Mal d 1), apricot (Pru ar 1), hazelnut (Cor a 1) and other vegetable sources, Vieths et al. (2002) [587] suggested that Pru ar 1 is involved in IgE cross-reactive allergies. In most cases Bet v 1 seems to be the sensitizing agent.
        • Allergen properties & biological function:This allergen is likely to be a pathogenesis-related protein and may have a role in plant protection against insect pests and microbial pathogens. However its precise function is not known.
        • Allergen purification:Not reported
        • Other biochemical information:

        References (2)

        • Didier Mbeguie-A-Mbeguie, Rose-Marie Gomez, and Bernard Fils-Lycaon
          Sequence of an Allergen-, Stress-, and Pathogenesis-related Protein From Apricot Fruit (Accession No. U93165). Gene Expression During Fruit Ripening. (PGR97-180).
          Plant Physiol. 115: 1730. 1997
          PUBMEDID:
        • Vieths S, Scheurer S, Ballmer-Weber B.
          Current understanding of cross-reactivity of food allergens and pollen.
          Ann N Y Acad Sci. 964:47-68.. 2002
          PUBMEDID: 12023194

        Biochemical Information for Pru ar 3

        • Allergen Name:Pru ar 3
        • Alternatve Allergen Names:Non specific lipid transfer protein; LTP 1
        • Allergen Designation:Major
        • Protein Family:Protease inhibitor/seed storage/LTP family Pfam PF00234
        • Sequence Known?:Yes
        • Allergen accession No.s:P81651 :Swissprot: http://ca.expasy.org/cgi-bin/niceprot.pl?P81651
        • 3D Structure Accession No.:Not determined
        • Calculated Masses:9178 Da
        • Experimental Masses:9 kDa
        • Oligomeric Masses:
        • Allergen epitopes:Not known
        • Allergen stability:
          Process, chemical, enzymatic:

          Not known but likely to be thermostable and resistant to proteases as other members of the nsLTP family (Asero et al. 2000) [10]

        • Nature of main cross-reacting proteins:

          IgE to Pru ar 3 cross-reacts with LTP's from other Prunoideae (eg. peach). IgE binding to nsLTP from some pollens has been implicated (Garcia-Selles et al., 2002 [594]; Pastorello et al., 2000) [150] but the relationship between allergy to pollen and fruit nsLTPs has not been clearly defined

          Pru ar 3 has sequence identity to peach and almond LTPs of 91% and 94%, respectively (Conti et al. 2001) [38]

        • Allergen properties & biological function:Pru ar 3 has been identified as a nonspecific lipid transfer protein (ns LTP). Plant ns LTPs are thought to be involved in transport of fatty acids both intracellular and extracellularly and of cutin monomers to the cuticular layer of leaves and fruits. There is an expandable cavity between the four alpha-helices which can bind one or two lipids. nsLTPs have also been reported to act as plant defense proteins against bacterial and fungal infections and form the PR14 family of pathogenesis related proteins. (Lindorff-Larsen et al. 2001 [903]).
        • Allergen purification:Pru ar 3 was purified by cation-exchange chromatography using a Resource-S column. The gradient length was 20 column volumes, with a flow rate of 6 mL/min. Gel filtration Superdex 75 column equilibrated and eluted with 50 mmol/L sodium acetate 3-hydrate at a flow rate of 0.7 mL/min was used (Pastorello et al. 2000) [150].
        • Other biochemical information:

        References (5)

        • García Sellés FJ, Diaz-Perales A, Sanchez-Monge R, Alcantara M, Lombardero M, Barber D, Salcedo G, Fernandez-Rivas M
          Patterns of reactivity to lipid transfer proteins of plant foods and Artemisia pollen: an in vivo study
          Int Arch Allergy Immunol. 128(2):115-122. 2002
          PUBMEDID: 12065911
        • Conti A; Fortunato D; Ortolani C; Giuffrida MG; Pravettoni V; Napolitano L; Farioli L; Garoffo LP; Trambaioli C; Pastorello EA
          Determination of the primary structure of two lipid transfer proteins from apricot (Prunus armeniaca)
          JOURNAL OF CHROMATOGRAPHY B 756, Iss 1-2, pp 123-129. 2001
          PUBMEDID: 11419703
        • Pastorello EA, D'Ambrosio FP, Pravettoni V, Farioli L, Giuffrida G, Monza M, Ansaloni R, Fortunato D, Scibola E, Rivolta F, Incorvaia C, Bengtsson A, Conti A, Ortolani C
          Evidence for a lipid transfer protein as the major allergen of apricot.
          J Allergy Clin Immunol 105:371-377. 2000
          PUBMEDID: 10669861
        • Asero R, Mistrello G, Roncarolo D, de Vries SC, Gautier MF, Ciurana CL, Verbeek E, Mohammadi T, Knul-Brettlova V, Akkerdaas JH, Bulder I, Aalberse RC, van Ree R.
          Lipid transfer protein: a pan-allergen in plant-derived foods that is highly resistant to pepsin digestion.
          Int Arch Allergy Immunol. 122:20-32.. 2000
          PUBMEDID: 10859466
        • Lindorff-Larsen K, Lerche MH, Poulsen FM, Roepstorff P, Winther JR.
          Barley lipid transfer protein, LTP1, contains a new type of lipid-like post-translational modification.
          J Biol Chem. 276(36):33547-33553.. 2001
          PUBMEDID: 11435437