f421 rPru p 4 Profilin, Peach

Allergens within Food of Plant Origin

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  • Common names: Profilin
  • Source material: An E. coli strain carrying a cloned cDNA encoding Prunus persica allergen Pru p 4.

Allergen
rPru p 4 (2).

Biological function:
Actin-binding protein.

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 4, a Peach profilin, 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 (38). 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 (39). They are heat- and dIgE antibodiesstion-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 (40). 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 (41).

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) (42).

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 specific 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, 43-44). Melon profilin has been shown to have substantial cross-reactivity with the Peach, Tomato, Grape and Bermuda grass (Cynodon dactylon) pollen profilins (41).

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 (45).

Compiled by Dr Harris Steinman, harris@zingsolutions.com

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2008



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