rPru p 1 PR-10, Peach

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Code: f419
Latin name: Prunus persica
Source material: rPru p 1 is a CCD-free recombinant protein
Common names: Group 1 Fagales-related Protein.

Peach allergen components

Available ImmunoCAP®:


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


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