rPru p 1 PR-10, Peach

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Code: f419
Latin name: Prunus persica
Common names: Group 1 Fagales-related Protein.

Peach allergen components

Available ImmunoCAP®:

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, PR-10 protein.
  • Pru p 3, a non-specific 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 non-specific lipid transfer proteins (nsLTPs) (35). Allergic symptoms involving nsLTPs 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).


Allergens from Prunus persica listed by IUIS*

Pru p 1 Pru p 3 Pru p 4

*International Union of Immunological Societies (www.allergen.org) Jan. 2008.



f419 rPru p 1

Recombinant non-glycosylated protein produced in an E. coli strain strain carrying a cloned cDNA encoding Prunus persica allergen Pru p 1

Common name: Bet v 1-homologous allergen, Group 1 Fagales-related protein, PR-10 protein
Biological function: Ribonuclease
Mw: 17 kDa

Allergen description

Pru p 1 is a 17 kDa peach protein belonging to the PR-10 protein family. The major birch pollen allergen Bet v 1 is the most prominent member of this family, with which Pru p 1 shares 59% amino acid sequence identity (40). In some allergen sources, PR-10 like proteins have been shown to be encoded by multiple genes, giving raise to arrays of closely related isoforms. Further, PR-10 proteins are produced intracellularly in a tissuedependent manner during plant development and their expression is subject to regulation by factors such as environmental stress or pathogen attack (41). The threedimensional structure of several PR-10 protein has been determined and found to contain a solvent-exposed cavity in which ligands such as fatty acids, brassicosteroids or phospholipids may bind (42-43).

Pru p 1 is heat labile (44-45) and most subjects suffering from birch pollen induced peach allergy may therefore tolerate food items containing cooked peaches.

The concentration of Pru p 1 in peach fruit is low (46). In addition Pru p 1 is easily degraded and/or chemically modified during extraction procedures and may thus be inadequately represented in natural peach extracts (47).

PR-10 proteins have been identified in many plant foods as well as in pollen of Fagales species (e.g. birch, hazel, alder, oak, hornbeam, beech). Despite relatively modest levels of sequence identity, homologues from more distantly related plant species, such as Pru av 1 from cherry and Api g 1 from celery, are structurally similar (48-49) which explains the observed cross-reactivity patterns within the protein family. Pru p 1 cross-reacts extensively with Bet v 1 homologous from Prunus pecies (e.g. cherry, apricot, plum) and other Roseaceae fruits such as apple and also, although to a lower degree, with PR-10 proteins from foods like carrot, celery, soy and peanut.

While Pru p 1 is the vastly predominant allergen in birch pollen-related peach allergy, IgE reactivity to Pru p 1 is less common among peach allergic subject in birch-free areas such as many Mediterranean regions.

Sensitization to Pru p 1 is not necessarily manifested as clinical reactions to peach but is a good marker for the birch-fruit syndrome.

Ingestion of peach and other related foods may elicit local reactions such as the oral allergy syndrome (OAS) and rhino-conjuctivitis but also, in rare cases, more severe systemic reactions (37-39).

f420 rPru p 3

Recombinant non-glycosylated protein produced in an E. coli strain strain carrying a cloned cDNA encoding Prunus persica allergen Pru p 3

Common name: nsLTP 2
Biological function: Non-specific lipid transfer protein
Mw: 9-10 kDa

Allergen description

Pru p 3 is a non-specific lipid transfer protein (nsLTP). nsLTPs are panallergens that have a ubiquitous distribution in tissues of many plant species, resulting in variable degrees of cross-reactivity, and in particularly relevant cross-reactivity in fruits and vegetables (23).

Lipid transfer proteins are small molecules of approximately 9 -10 kDa that demonstrate great stability and are very resistant to pepsin and heat treatment (50). Lipid transfer proteins facilitate the transport of phospholipids and galactolipids across membranes. Non-specific lipid transfer proteins belong to the PR 14 family of pathogenesis-related proteins.

Lipid transfer proteins are highly conserved and widely distributed throughout the plant kingdom. They have been identified as allergens in the Rosaceae subfamilies of the Prunoideae (Peach, Apricot, Plum) and of the Pomoideae (Apple). They belong to a family of structurally highly conserved proteins that are also present in non-Rosaceae vegetable foods. They have been linked to severe and systemic symptoms and induce sensitisation by the oral route in fruit-allergic patients who do not have associated pollen allergy. This is probably due to extreme pepsin stability; the allergens probably reach the intestinal tract in an almost unmodified form.

The lipid transfer proteins essentially concentrate in the skin of Rosaceae fruits as cell surface-exposed allergens (15, 28). LTP is found in Peach peel in amounts approximately 7 times greater than in pulp (26). It may be absent from chemically peeled fruit, and levels of LTP vary in different cultivars and at different stages of the ripening process, showing a progressive increment during ripening (51). A study was made to evaluate the hypothesis that Peach may lose its allergenicity and therefore its primary role as a sensitiser to LTP as a consequence of processing preceding marketing in Northern Europe: Peach surface fuzz reactivity in Peach-allergic individuals was shown to be stronger than reactivity to peel. Pre-absorption of one serum with Peach LTP caused an 87% reduction of IgE antibodies reactivity to Peach fuzz extract (35).

Allergy to lipid transfer protein is quite common in the Mediterranean countries but almost absent in Northern Europe (35). Lipid transfer protein is usually associated with more severe systemic reactions than oral allergy syndrome. Peach LTP (Pru p 3) is a minor allergen in Northern European countries but a major allergen in the South, affecting over 60% of patients allergic to Peach in the Spanish population (1). In Peach-allergic patients who have experienced systemic reactions to Peach, up to 100% may be sensitised to LPT (17).

Pru p 3, possibly along with other larger proteins, is involved in allergenic relationships with other fruits from the family Rosaceae, particularly Apricot, Cherry, and Plum (15-16,52). A high level of cross-reactivity occurs among fruits and vegetables containing lipid transfer proteins, which include Sweet chestnut (53), Cabbage (with 50% identity to Peach LTP) (54), Walnut (55), Lettuce (56), and Hazelnut (57). Grape and wine may contain lipid transfer protein homologous to and cross-reactive with Peach LTP (58). A report was made on a 19-year-old boy with a history of oral allergy syndrome after eating Peach, who presented with several episodes of generalised urticaria and angioedema approximately 15-20 minutes after drinking beer. It was found that the responsible allergen was a lipid transfer protein from Barley that was present in beer (59). Lipid transfer protein cross-reactivity is often accompanied by clinical food allergy, frequently including systemic reactions (22).

In a study examining the relationship between Peach LTP-specific IgE antibodies levels and cross-reactivity to several non-Rosaceae plant-derived foods, patients with negative skin reactivity for non-Rosaceae foods showed significantly lower levels of IgE antibodies to Peach LTP than did patients showing skin reactivity to one or more non-Rosaceae foods. Increasing levels of IgE antibodies to Peach LTP were associated with skin reactivity to nuts (29/40 [72%]), Peanut (27/40 [67%]), Maize (16/39 [41%]), Rice (14/39 [36%]), Onion (13/37 [35%]), Orange (9/32 [28%]), Celery (11/40 [27%]), and Tomato (8/39 [20%]). The study suggested that all allergenic determinants in LTP from vegetable foods other than Peach cross-react with Peach LTP determinants, whereas only some Peach LTP epitopes cross-react with allergenic determinants on botanically unrelated plant-derived foods. The high levels of IgE antibodies to Peach LTP suggested the presence of IgE antibodies that targeted common allergenic determinants of LTP, causing cross-reactivity to botanically unrelated vegetable foods. The authors concluded that in LTP-allergic patients, increasing levels of IgE antibodies to Peach LTP are paralleled by an increasing number of foods other than Rosaceae that are positive on skin test and cause clinical symptoms (60).

Allergenic LTPs from Peach fruit and Mugwort (Artemisia vulgaris) pollen are responsible for clinical symptoms in Mediterranean patients as a result of cross-reactivity (53, 61). In a study assessing the pattern of sensitisation to an array of Mugwort allergens in a Mediterranean population and the cross-reactivity of Art v 3 (Mugwort) with Pru p 3 and Par j 1, relevant lipid transfer proteins (LTP) allergens in the area, the 3 Artemisia allergens elicited a positive skin reactivity in 70 to 80% of the patients. Seven patients were clearly sensitised to Par j 1 and 11 to Pru p 3. There was no correlation between Par j 1 and Pru p 3 sensitisation, but a highly significant correlation was found between Peach and Art v 3 with regard to skin reactivity. No IgE antibodies cross-reactivity was observed between Art v 3 and Par j 1, or between Pru p 3 and Par j 1. In contrast, Art v 3 significantly inhibited the binding to Pru p 3 of IgE antibodies from 3 patients’ sera out of 6 studied, but Pru p 3 was not able to inhibit IgE antibodies binding to Art v 3. The study concludes that Art v 3 is a major Mugwort allergen, and that in some patients with IgE antibodies to both Art v 3 and Pru p 3, Art v 3 behaves as the primary sensitising agent (62).

Therefore, hypersensitivity to Mugwort in patients with Peach allergy is due to a common lipid transfer protein allergen and is often without clinical expression (63). This is illustrated by a study of 47 patients allergic to Peach and 20 patients sensitised to Mugwort pollen who had no clinical food allergies; the rate of positive skin test for Peach, Apple, Chestnut and Mugwort LTPs were, respectively, 91, 77, 23, and 36% in the Peach group, and 30, 5, 15 and 40% in the Artemisia group. In Peach-allergic patients, the most frequent pattern of cross-reactivity to LTPs appears to be the combination Peach-Apple (45%), followed by Peach-Apple-Mugwort-Sweet chestnut (21%). Significant correlation was found between Peach and Apple LTPs, and between Mugwort and Sweet Chestnut LTPs (4).

It has been suggested that the primary sensitiser to LTP is Peach (35). Cross-reactivity to non-Rosaceae vegetable foods is strongly dependent on the level of IgE antibodies to Peach LTP (35,60).

In a study, immunodetection and immunoblot inhibition assays were carried out with sera from Peach-allergic patients and demonstrated that both the recombinant and natural forms of Pru p 3 displayed similar IgE antibodies-binding capacity (25).

In a study of 10 patients with allergy to Peach, all having experienced systemic reactions to Peach, all 10 patients had positive skin responses to nPru p 3, and 9 of 10 patients had positive FAST and CAST responses both with nPru p 3 and rPru p 3. Histamine release test responses were considered positive in 5 and 7 patients for nPru p 3 and rPru p 3, respectively. The study concluded that recombinant Pru p 3 showed a strong immunologic activity equivalent to that of its natural counterpart (17).


f421 rPru p 4

Recombinant non-glycosylated protein produced in an E. coli strain strain carrying a cloned cDNA encoding Prunus persica allergen Pru p 4

Biological function: Profilin
Mw: 14 kDa

Allergen description

Pru p 4, a Peach profilin and an actinbinding protein, is a member of the profilin plant family. Profilins are panallergens that are recognised by IgE antibodies of about 20% of patients allergic to Birch pollen and plant foods (64). However, sensitisation to profilin can be expected in different populations at levels varying between 5 and 40%, depending on exposure to various profilin-containing allergen sources (65). They are heat- and digestion-labile and are therefore more often associated with less severe allergic reactions and oral allergy syndrome.

Profilins are small eukaryotic proteins, 14 - 17 kDa in size, involved in modulating the assembly of actin microfilaments in the cytoplasm. Profilins are ubiquitous in all eukaryotic organisms. They are able to bind both phosphatidylinositol-4,5-bisphosphate and poly-L-proline (PLP) and thus play a critical role in signaling pathways. Plant profilins are of particular interest because immunological cross-reactivity between pollen and human profilin may be the cause of hay fever and broad allergies to pollens (66). IgE antibodies reactivity to profilin appears to strongly depend on the highly conserved conformational structure, rather than on a high degree of amino acid sequence identity or even linear epitopes identitied, as demonstrated in a study evaluating Melon profiling (67).

Profilins can be isolated from tree pollens, e.g., Birch tree (Betula verrucosa), from pollens of grasses, e.g., Timothy grass (Phleum pratense), and from pollens of weeds, e.g., Mugwort (Artemisia vulgaris) (67).

Peach contains 2 profilin isoforms, Pru p 4.01 and Pru p 4.02, which show 80% amino acid sequence identity and are very similar (>70% identity) to allergenic profilins from plant foods and pollens. A complete correlation between reactivity to rPru p 4 and to rBet v 2 has been found in sera from Peach-allergic patients. In a study evaluating recombinant Peach profilin isoform reactivity, using sera of 29 patients with Peach allergy (as proved by DBPCFC), Pru p 4.01 was recognised by all sera (15 of 15) with IgE antibodies to Bet v 2, whereas no sera (0 of 14) without IgE antibodies to Birch allergen reacted with rPru p 4.01 (2). In the Spanish population, where Peach LTP is a major allergen, sensitisation to profilin is observed to be connected to pollen allergy but does not appear to be related to clinical reactivity to Peach (1). This may also be observed in other countries, in particular in Southern Europe, where Peach LPT is the dominant allergen.

IgE antibodies antibodies to profilin seem to be responsible for at least part of the observed allergenic relationship between Peach and grass and Olive tree pollen in the Mediterranean area, where Betulaceae pollens in the air are rare or absent (11,32, 68-70). Melon profilin has been shown to have substantial cross-reactivity with the Peach, Tomato, Grape and Bermuda grass (Cynodon dactylon) pollen profilins (67).

Some studies suggest partial or even absent IgE antibodies cross-reactivity among certain profilins. A study reports that the large amount of cross-reactivity among plant profilins justifies using a single profilin for diagnosis. However, it should be kept in mind that the fine specificity of IgE antibodies directed to variable epitopes may influence the clinical manifestation of profilin sensitisation (71).

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;380:1315-20
  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. 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):535-42
  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):118-21
  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. Gamboa PM, et al. Two different profiles of peach allergy in the north of Spain.
    Allergy 2007;Apr62(4):408-14
  38. Fernádez-Rivas M, et al. Apple allergy across Europe: how allergen sensitization profiles determine the clinical expression of allergies to plant foods. J Allergy Clin Immunol 2006;Aug118(2):481-8
  39. Asero R. Plant food allergies: a suggested approach to allergenresolved diagnosis in the clinical practice by identifying easily available sensitization markers. Int Arch Allergy Immunol 2005;Sep138(1):1-11
  40. Marknell Dewitt, Å, Andersson K, Lidholm J. Cloning and sequence of the major peach allergen Pru p 1. Sequence Accession No. ABB78006, direct submission.
  41. Hoffmann-Sommergruber, K. Pathogenesis-related (PR)-proteins identified as allergens. Biochemical Society Transactions 2002;30(Pt 6):930-5
  42. Markovic-Housley Z., et al. Crystal structure of a hypoallergenic isoform of the major birch pollen allergen Bet v 1 and its likely biological function as a plant steroid carrier. Journal of Molecular Biology 2003;325(1):123-33
  43. Mogensen J, et al. The major birch allergen, Bet v 1, shows affinity for a broad spectrum of physiological ligands. Journal of Biological Chemistry 2002;277(26):23684-92
  44. Scheurer S, et al. Strong allergenicity of
    Pru av 3, the lipid transfer protein from cherry, is related to high stability against thermal processing and digestion. Journal of Allergy & Clinical Immunology 2004;114(4):900-7
  45. Vieths S, Scheurer S, Ballmer-Weber B. Current Understanding of Cross-Reactivity of Food Allergens and Pollen. Annals of the New York Academy of Sciences 2002;964:47-68
  46. Ahrazem O, et al. Assessing allergen levels in peach and nectarine cultivars. Ann Allergy Asthma Immunol 2007;99(1):42-7
  47. Asero R, et al. Allergy to nonspecific lipid transfer proteins in Rosaceae: a comparative study of different in vivo diagnostic methods. Ann Allergy Asthma Immunol 2001;87(1):68-71
  48. Neudecker P, et al. Mutational epitope analysis of Pru av 1 and Api g 1, the major allergens of cherry (Prunus avium) and celery (Apium graveolens): correlating IgE reactivity with three-dimensional structure. Biochemical Journal 2003;376(Part 1):97-107
  49. Neudecker P, et al. Allergic cross-reactivity made visible – Solution structure of the major cherry allergen Pru av 1.
    Journal of Biological Chemistry 2001;276(25):22756-63
  50. Asero R, Amato S, Alfieri B, Folloni S, Mistrello G. Rice: Another potential cause of food allergy in patients sensitized to lipid transfer protein. Int Arch Allergy Immunol 2007;143(1):69-74
  51. Brenna OV, Pastorello EA, Farioli L, Pravettoni V, Pompei C. Presence of allergenic proteins in different peach (Prunus persica) cultivars and dependence of their content on fruit ripening.
    J Agric Food Chem 2004;52(26):7997-8000
  52. Scheurer S, Pastorello EA, Wangorsch A, Kastner M, Haustein D, Vieths S. Recombinant allergens Pru av 1 and Pru av 4 and a newly identified lipid transfer protein in the in vitro diagnosis of cherry allergy.
    J Allergy Clin Immunol 2001;107(4):724-31
  53. Sanchez-Monge R, Blanco C, Lopez-Torrejon G, Cumplido J, Recas M, Figueroa J, Carrillo T, Salcedo G. Differential allergen sensitization patterns in chestnut allergy with or without associated latex-fruit syndrome.
    J Allergy Clin Immunol 2006;118(3):705-10
  54. Palacin A, Cumplido J, Figueroa J, Ahrazem O, Sanchez-Monge R, Carrillo T, Salcedo G, Blanco C. Cabbage lipid transfer protein Bra o 3 is a major allergen responsible for cross-reactivity between plant foods and pollens. J Allergy Clin Immunol 2006;117(6):1423-9
  55. Pastorello EA, Farioli L, Pravettoni V, Robino AM, Scibilia J, Fortunato D, Conti A, Borgonovo L, Bengtsson A, Ortolani C. Lipid transfer protein and vicilin are important walnut allergens in patients not allergic to pollen. J Allergy Clin Immunol 2004;114(4):908-14
  56. San Miguel-Moncin M, Krail M, Scheurer S, Enrique E, Alonso R, Conti A, Cistero-Bahima A, Vieths S. Lettuce anaphylaxis: identification of a lipid transfer protein as the major allergen. Allergy 2003;58(6):511-7
  57. Pastorello EA, Vieths S, Pravettoni V, Farioli L, Trambaioli C, et al. Identification of hazelnut major allergens in sensitive patients with positive double-blind, placebo-controlled food challenge results.
    J Allergy Clin Immunol 2002;109(3):563-70
  58. Pastorello EA, Farioli L, Pravettoni V, Ortolani C, Fortunato D, Giuffrida MG, Perono Garoffo L, Calamari AM, Brenna O, Conti A. Identification of grape and wine allergens as an endochitinase 4, a lipid-transfer protein, and a thaumatin.
    J Allergy Clin Immunol 2003;111(2):350-9
  59. Asero R, Mistrello G, Roncarolo D, Amato S, van Ree R. A case of allergy to beer showing cross-reactivity between lipid transfer proteins. Ann Allergy Asthma Immunol 2001;87(1):65-7
  60. Asero R, Mistrello G, Roncarolo D, Amato S. Relationship between peach lipid transfer protein specific IgE antibodies levels and hypersensitivity to non-Rosaceae vegetable foods in patients allergic to lipid transfer protein. Ann Allergy Asthma Immunol 2004;92(2):268-72
  61. Egger M, Mutschlechner S, Wopfner N, Gadermaier G, Briza P, Ferreira F. Pollen-food syndromes associated with weed pollinosis: an update from the molecular point of view. Allergy 2006;61(4):461-76
  62. Lombardero M, Garcia-Selles FJ, Polo F, Jimeno L, Chamorro MJ, Garcia-Casado G, Sanchez-Monge R, Diaz-Perales A, Salcedo G, Barber D. Prevalence of sensitization to Artemisia allergens Art v 1, Art v 3 and Art v 60 kDa. Cross-reactivity among Art v 3 and other relevant lipid-transfer protein allergens. Clin Exp Allergy 2004;34(9):1415-21
  63. Pastorello EA, Pravettoni V, Farioli L, Rivolta F, Conti A, Ispano M, Fortunato D, Bengtsson A, Bianchi M. Hypersensitivity to mugwort (Artemisia vulgaris) in patients with peach allergy is due to a common lipid transfer protein allergen and is often without clinical expression. J Allergy Clin Immunol 2002;110(2 Pt 1):310-7
  64. Willerroider M, Fuchs H, Ballmer-Weber BK, Focke M, Susani M, Thalhamer J, Ferreira F, Wuthrich B, Scheiner O, Breiteneder H, Hoffmann-Sommergruber K. Cloning and molecular and immunological characterisation of two new food allergens, Cap a 2 and Lyc e 1, profilins from Bell pepper (Capsicum annuum) and Tomato (Lycopersicon esculentum). Int Arch Allergy Immunol 2003;131(4):245-55
  65. Elfman L, Svensson M, Lidholm J, Pauli G, Valenta R. Different profiles in specific IgE antibodies to rBet v 1 and rBet v 2 in patients allergic to birch pollen from six countries. Int Arch Allergy Immunol 1997;113(1-3):249-51
  66. Thorn KS, Christensen HE, ShIgE antibodiesta R, Huddler D, Shalaby L, Lindberg U, Chua NH, Schutt CE. The crystal structure of a major allergen from plants. Structure 1997;5(1):19-32
  67. Sankian M, Varasteh A, Pazouki N, Mahmoudi M. Sequence homology: A poor predictive value for profilins cross-reactivity. Clin Mol Allergy 2005;3(1):13
  68. Valenta R, Duchene M, Ebner C, et al. Profilins constitute a novel family of functional plant pan-allergens.
    J Exp Med 1992;175:377-85
  69. Cuesta-Herranz J, Lazaro M, Martinez A, Figueredo E, Palacios R, de-Las-Heras M, Martinez J. Pollen allergy in peach-allergic patients: sensitization and cross-reactivity to taxonomically unrelated pollens. J Allergy Clin Immunol 1999;104(3 Pt 1):688-94
  70. Wensing M, Akkerdaas JH, Van Leeuwen WA, Stapel SO, Bruijnzeel-Koomen CA, Aalberse RC, Bast BJ, Knulst AC, Van Ree R. IgE antibodies to Bet v 1 and profilin: Cross-reactivity patterns and clinical relevance.
    J Allergy Clin Immunol 2002;110(3):435-42
  71. Radauer C, Willerroider M, Fuchs H, Hoffmann-Sommergruber K, Thalhamer J, Ferreira F, Scheiner O, Breiteneder H. Cross-reactive and species-specific immunoglobulin E epitopes of plant profilins: an experimental and structure-based analysis.
    Clin Exp Allergy 2006;36(7):920-9

As in all diagnostic testing, the diagnosis is made by the physican based on both test results and the patient history.