f419 rPru p 1 PR-10, Peach

Allergens within Food of Plant Origin

Print Print icon Tell a friend Tell a friend icon
  • Latin name: Prunus persica
  • Common names: Group 1 Fagales-related Protein.
  • Source material: An E. coli strain carrying a cloned cDNA encoding the Prunus persica allergen Pru p 1.

Biological function
A ribonuclease.

Mw:
Approximately 14 kDa

Summary
Peach is the fruit of a small deciduous tree growing to 10 m tall, belonging to the subfamily Prunoideae of the family Rosaceae. It is classified with the Almond in the subgenus Amygdalus within the genus Prunus, distinguished from the other subgenera by the corrugated seed shell. Cultivated Peaches are divided into "freestone" and "clingstone" cultivars, depending on whether the flesh sticks to the stone or not. These two classes merge in different varieties, and even the same variety of tree may yield freestone and clingstone fruit in different seasons. Both kinds can have either white or yellow flesh. At least 300 varieties of Peach are grown throughout the world, each with distinct physical characteristics and a distinct ripening season.

The nectarine is a cultivar of Peach that has a smooth skin without fuzz (hair). Nectarines can be white, yellow, clingstone, or freestone. Regular Peach trees occasionally produce a few nectarines, and vice versa. Peaches and nectarines look very similar, but they can be told apart by their skin texture: Peaches are fuzzy and dull, while nectarines are smooth and shiny.

Peach is a well-documented and common cause of allergy in children and adults, resulting in oral allergy and systemic reactions such as urticaria, asthma and anaphylactic shock following the ingestion of fresh or processed fruit. This is particularly notable in the Mediterranean area, where Peach is regarded as a major allergen (1-14). Peach has also been described as the primary food causing anaphylaxis in Israel (12).

Several Peach allergens of major importance have been detected, including a lipid transfer protein, a profilin, and many larger proteins (15-16).

The following allergens have been characterised.

  • Pru p 1, a Group 1 Fagales-related Protein.
     
  • Pru p 3, a 9 kDa lipid transfer protein (1, 15-31).
     
  • Pru p 4, a Profilin (16-17, 20, 32).
     
  • Pru p glucanase, a 1,3-beta-glucanase (33-34).

The allergen that was known as Pru p 1 has been renamed Pru p 3, and Pru p 1 is now the name for a PR10 protein, the Group 1 Fagales-related Bet v 1 homologue.

Peach-allergic individuals in the Mediterranean area are in most cases not allergic to Birch tree pollen, and the main reactions are not directed to Bet v 1 homologues or profilin but to LTPs (35). Allergic symptoms involving LTPs are more likely to be systemic and severe, in addition to causing oral allergy syndrome. In contrast, sensitisation to the lipid transfer protein Pru p 3 is rare among Central and Northern European populations (17).  Morever, allergy to Peach and other Rosaceae fruits in patients with a related pollen allergy, like most patients in these populations, is a milder clinical entity, and profilin- and Bet v 1-related structures are involved (36).

Recombinant allergens, which are genetically engineered isoforms resembling allergen molecules from known allergen extracts, have immunoglobulin E (IgE antibodies) antibody binding comparable to that of natural allergens and generally show excellent reactivity in in vitro and in vivo diagnostic tests (37). To date, many different recombinant allergens of various pollens, molds, mites, and foods, as well as latex and bee venom, have been cloned, sequenced, and expressed.

Recombinant allergens have a wide variety of uses, from the diagnosis and management of allergic patients to the development of immunotherapy to the standardisation of allergenic test products as tools in molecular allergology research to elucidate the molecular mechanisms underlying the allergic reactions. Recombinant allergens are particularly useful for investigations of allergies manifesting wide cross-reactivity. However, recombinant allergens may be inaccurately processed and folded and thus show a different allergenic expression than their natural counterparts do. Therefore, a prerequisite for the use of recombinant forms is ensuring that their physicochemical and immunologic properties are equivalent to those of their natural counterparts (17).
 

Allergen description
Pru p 1, a Group 1 Fagales-related Protein (a Bet v 1 homologue), is a common protein found in a number of plants and recognised as a panallergen (16). The allergen that previously was known as Pru p 1 has been renamed Pru p 3, and Pru p 1 is now the name for a Group 1 Fagales-related Protein, a Bet v 1 homologue.

Allergy to fruits and vegetables is often associated with pollen allergy, but the relationship between fruit and pollen allergens is not simple. Cross-reactivity patterns observed differs among geographical areas and climates, depending on the differences in exposure to inhaled and ingested allergens. For example, the association between Birch tree pollen allergy and Peach food allergy in northern Europe (8) may be explained by the detection of a Bet v 1-related protein in Peach (16), whereas in Southern Europe, cross-reactivity associated with Peach is more likely to be connected with allergy to other fruits and vegetables containing lipid transfer proteins (35). Cross-reactivity between Peach and other plants containing Bet v 1-homologous allergens is possible.

Compiled by Dr Harris Steinman, harris@zingsolutions.com

References:

    1. Fernandez-Rivas M, Gonzalez-Mancebo E, Rodriguez-Perez R, Benito C, Sanchez-Monge R, Salcedo G, Alonso MD, Rosado A, Tejedor MA, Vila C, Casas ML. Clinically relevant peach allergy is related to peach lipid transfer protein, Pru p 3, in the Spanish population. J Allergy Clin Immunol 2003;112(4):789-95
    2. Rodriguez-Perez R, Fernandez-Rivas M, Gonzalez-Mancebo E, Sanchez-Monge R, Diaz-Perales A, Salcedo G. Peach profilin: cloning, heterologous expression and cross-reactivity with Bet v 2. Allergy 2003;58(7):635-40
    3. 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 2000;106(1 Pt 1):183-9
    4. Garcia-Selles FJ, Diaz-Perales A, Sanchez-Monge R, Alcantara M, et al. Patterns of reactivity to lipid transfer proteins of plant foods and Artemisia pollen: an in vivo study.: An in vivo Study. Int Arch Allergy Immunol 2002;128(2):115-22
    5. Bircher AJ, Van Melle G, Haller E, Curty B, Frei PC. IgE antibodies to food allergens are highly prevalent in patients allergic to pollens, with and without symptoms of food allergy. Clin Exp Allergy 1994;24(4):367-74
    6. Ortolani C, Ispano M, Pastorello E, Bigi A, Ansaloni R. The oral allergy syndrome. Ann Allergy 1988;61(6 Pt 2):47-52.
    7. Amat Par P, Sanosa Valls J, Lluch Perez M, Malet Casajuana A, Garcia Calderon PA. Dried fruit hypersensitivity and its correlation with pollen allergy. Allergol Immunopathol (Madr) 1990;18(1):27-34.
    8. Eriksson NE. Food sensitivity reported by patients with asthma and hay fever. A relationship between food sensitivity and birch pollen-allergy and between food sensitivity and acetylsalicylic acid intolerance. Allergy 1978;33(4):189-96.
    9. de Groot H, de Jong NW, Vuijk MH, Gerth van Wijk R. Birch pollinosis and atopy caused by apple, peach, and hazelnut; comparison of three extraction procedures with two apple strains. Allergy 1996;51(10):712-8
    10. Guillet MH, Guillet G. Food urticaria in children. Review of 51 cases. [French]. Allerg Immunol (Paris) 1993;25(8):333-8.
    11. Cuesta-Herranz J, Lazaro M, de las Heras M, et al. Peach allergy pattern: experience in 70 patients. Allergy 1998;53(1):78-82.
    12. Kivity S, Dunner K, Marian Y. The pattern of food hypersensitivity in patients with onset after 10 years of age. Clin Exp Allergy 1994;24(1):19-22.
    13. Crespo JF, Rodriguez J, James JM, Daroca P, Reano M, Vives R. Reactivity to potential cross-reactive foods in fruit-allergic patients: implications for prescribing food avoidance. Allergy 2002;57(10):946-9
    14. Malet A, Sanosa J, et al. Diagnosis of allergy to peach. A comparative study of "in vivo" and "in vitro" techniques. Allergol Immunopathol (Madr) 1988;16(3):181-4
    15. Lleonart R, Cistero A, Carreira J, Batista A, Moscoso del Prado J. Food allergy: identification of the major IgE antibodies-binding component of peach (Prunus persica). Ann Allergy 1992;69(2):128-30.
    16. 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 1994;94(4):699-707
    17. Diaz-Perales A, Sanz ML, Garcia-Casado G, Sanchez-Monge R, Garcia-Selles FJ, Lombardero M, Polo F, Gamboa PM, Barber D, Salcedo G. Recombinant Pru p 3 and natural Pru p 3, a major peach allergen, show equivalent immunologic reactivity: a new tool for the diagnosis of fruit allergy. J Allergy Clin Immunol 2003;111(3):628-33
    18. Pastorello EA, Ortolani C, Baroglio C, et al. Complete amino acid sequence determination of the major allergen of peach (Prunus persica) Pru p 1. Biol Chem 1999;380:1315-1320
    19. van Ree R, Fernandez-Rivas M, Cuevas M, van Wijngaarden M, Aalberse RC. Pollen-related allergy to peach and apple: an important role for profilin. J Allergy Clin Immunol 1995;95(3):726-34.
    20. Pastorello EA, Incorvaia C, Pravettoni V, Farioli L, Conti A, Vigano G, Rivolta F, Ispano M, Rotondo F, Ortolani C New allergens in fruits and vegetables. Allergy 1998;53(46 Suppl):48-51
    21. Brenna O, Pompei C, Ortolani C, Pravettoni V, Farioli L, Pastorello EA. Technological processes to decrease the allergenicity of peach juice and nectar. J Agric Food Chem 2000;48(2):493-7
    22. Asero R, Mistrello G, Roncarolo D, de Vries SC, , Gautier MF, Ciurana CL, Verbeek E, Mohammadi T, Knul-Brettlova V, Akkerdaas JH, et al. Lipid transfer protein: a pan-allergen in plant-derived foods that is highly resistant to pepsin dIgE antibodiesstion. Int Arch Allergy Immunol 2000;122(1):20-32
    23. Sanchez-Monge R, Lombardero M, Garcia-Selles FJ, Barber D, Salcedo G. Lipid-transfer proteins are relevant allergens in fruit allergy. J Allergy Clin Immunol 1999;103(3 Pt 1):514-9
    24. International Union of Immunological Societies Allergen Nomenclature: IUIS official list http://www.allergen.org/List.htm 2006
    25. Diaz-Perales A, Garcia-Casado G, Sanchez-Monge R, Garcia-Selles FJ, Barber D, Salcedo G. cDNA cloning and heterologous expression of the major allergens from peach and apple belonging to the lipid-transfer protein family. Clin Exp Allergy 2002;32(1):87-92
    26. 26 Carnes J, Fernandez-Caldas E, Gallego MT, Ferrer A, Cuesta-Herranz J. Pru p 3 (LTP) content in peach extracts. Allergy 2002;57(11):1071-5
    27. Duffort OA, Polo F, Lombardero M, Diaz-Perales A, Sanchez-Monge R, Garcia-Casado G, Salcedo G, Barber D. Immunoassay to quantify the major peach allergen Pru p 3 in foodstuffs. Differential allergen release and stability under physiological conditions. J Agric Food Chem 2002;50(26):7738-41
    28. Borges JP, Jauneau A, Brule C, Culerrier R, Barre A, Didier A, Rouge P The lipid transfer proteins (LTP) essentially concentrate in the skin of Rosaceae fruits as cell surface exposed allergens. Plant Physiol Biochem 2006;44(10):535-542
    29. Pasquato N, Berni R, Folli C, Folloni S, Cianci M, Pantano S, Helliwell JR, Zanotti G. Crystal structure of peach Pru p 3, the prototypic member of the family of plant non-specific lipid transfer protein pan-allergens. J Mol Biol 2006;356(3):684-94.
    30. Zuidmeer L, van Leeuwen WA, Kleine B, Cornelissen J, Bulder I, Rafalska I, Tellez BN, Akkerdaas JH, Asero R, Fernandez RM, Gonzalez ME, van RR. Lipid Transfer Proteins from Fruit: Cloning, Expression and Quantification. Int Arch Allergy Immunol 2005;137(4):4-281
    31. Pastorello EA, FPastorello EA, Farioli L, Pravettoni V, Ortolani C, Ispano M, Monza M, Baroglio C, Scibola E, Ansaloni R, Incorvaia C, Conti A. The major allergen of peach (Prunus persica) is a lipid transfer protein. J Allergy Clin Immunol 1999;103(3 Pt 1):520-6
    32. Daschner A, Crespo JF, Pascual CY. Specific IgE antibodies to recombinant vegetal panallergen (rBet v 2) and fruit allergy in pollinic patients. Allergy 1998;53(6):614-8.
    33. Barral P, Batanero E, Palomares O, Quiralte J, Villalba M, Rodriguez R. A major allergen from pollen defines a novel family of plant proteins and shows intra- and interspecies [correction of interspecie] cross-reactivity. J Immunol 2004;172(6):3644-51.
    34. Thimmapuram J, Ko TS, Korban SS. Characterization and expression of beta-1,3-glucanase genes in peach. Mol Genet Genomics 2001;265(3):469-79.
    35. Asero R, Mistrello G, Amato S, Roncarolo D, Martinelli A, Zaccarini M. Peach fuzz contains large amounts of lipid transfer protein: is this the cause of the high prevalence of sensitization to LTP in Mediterranean countries? Allerg Immunol (Paris) 2006;38(4):118-121
    36. Fernandez Rivas M, van Ree R, Cuevas M. Allergy to Rosaceae fruits without related pollinosis. J Allergy Clin Immunol 1997;100(6 Pt 1):728-33
    37. Niederberger V, Stubner P, Spitzauer S, Kraft D, Valenta R, Ehrenberger K, Horak F. Skin test results but not serology reflect immediate type respiratory sensitivity: a study performed with recombinant allergen molecules. J Invest Dermatol 2001;117(4):848-51.

2008



Further Reading