Type:
Component
Allergen Encyclopedia
Table of Contents
Component
f419 Pru p 1
f419 Pru p 1 Scientific Information
Name; WHO/IUIS:
Pru p 1
Biological function:
PR-10 proteins, Ribonucleases
Allergen code:
f419
Molecular Weight:
18 kDa
Route of Exposure:
Ingestion
Source Material:
Peach
Other Names :
Group 1, Fagales-related protein, Pathogenesis-related protein, PR-10, Bet v 1 family member
Summary
The peach allergen, Pru p 1, is a pathogenesis-related (PR)-10 protein family member and shares a structure homology to the major birch pollen, Bet v 1. Thus, Pru p 1 sensitization is quite prevalent in areas with high exposure to birch pollen and typically results in oral allergy syndrome (oral itching, oral mucosa irritation, or angioedema of lips, tongue, or throat) symptoms. It is found to be sensitive to heat and gastrointestinal digestion. Pru p 1 can also cross-react with pollens such as grass or alder members and result in pollen-food allergy syndrome (PFAS). It can also cross-react with other members of Rosaceae family (apple, apricot, pear, cherry). Pru p 1 is one of the diagnostic indicators to detect allergy to Rosaceae family fruits.
Epidemiology
Worldwide distribution
Pru p 1 sensitivity is commonly found in parts of Northern and Central Europe which has high birch pollinosis due to the presence of cross-reactive IgE antibodies against Bet v 1 (major birch pollen allergen) (1). A study by Gaier et al. (2009) conducted on Austrian patients showed that 87% (47/54) patients had Pru p 1 sensitivity and 75.9% (41/54) patients were having birch pollen allergy. Besides, 6 of 47 Pru p 1 positive peach allergic patients were not having birch pollen allergy. (1). On the contrary, a prospective cross-sectional study among 57 children showed that sensitization to Pru p 1 is quite low (11% of 53) in Spain (part of Southern Europe) where birch pollen sensitized patients were less. Thus, Pru p 1 was found to be an important allergen in patients sensitized to birch pollen (2). Further, another study in Italy (part of Southern Europe) supported this sensitization pattern and found Pru p 1 sensitization in only 4 of 244 patients sensitized to peach (3).
Furthermore, another study evaluated the difference in sensitization pattern of Pru p 1 among 133 Pru p 3 positive patients from Northeast Italy and South Italy having a birch sensitization pattern like Northern Europe. Northeast patients sensitized to Pru p 1 were found to be 42.8% while none of the South Italy patients were sensitized towards Pru p 1 (4).
The prevalence of Pru p 1 sensitization was also found prevalent in Japanese peach allergic patients. It was found to be 91.7% among 12 patients showing oral or mucosal symptoms while 80% among 15 patients showing systemic symptoms including anaphylaxis (5). Another study in Japan among 50 patients also reported Pru p 1 sensitization to be 66% and mainly associated with oral and mucosal symptoms (6).
Pru p 1 sensitization was found to be 82.4% among the 51-birch pollen-sensitive patients in a study in Korea. The sensitization was found higher among the patients with OAS (7).
Environmental Characteristics
Source and tissue
Pru p 1 is a member of the PR-10 protein family and is present abundantly in the pulp and skin of peach fruit (8).
Clinical Relevance
Cross-reactive Molecules
Strong cross-reactivity exists between PR-10 allergens of peach (Pru p 1) and birch pollen (Bet v 1). Also, the prevalence of peach allergy is associated with birch pollinosis. The major symptoms manifested due to birch sensitivity include OAS (1). In a study in Austria on 35 Bet v 1-sensitized birch pollen allergic patients, peach allergy was found in 100% due to cross-sensitization to Pru p 1 (11).
Further, co-sensitization of peach allergy with alder or grass pollens allergy is also found and is related to PFAS (6). Further, alder pollen was proposed to be a primary sensitizer in peach allergic patients for their Pru p 1 and Pru p 4 sensitizations (5).
Disease severity
Clinical symptoms associated with Pru p 1 sensitivity usually affect the oral cavity and are often mild to moderate (9). These can be referred to as OAS.
A study in Japan showed that 94.2% of peach allergic patients (31/33) with Pru p 1 sensitivity developed oropharyngeal symptoms (p<0.005) (6).
A study conducted on 54 Austrian patients found that sensitization to Pru p 1 was significantly associated with reduced occurrence of urticaria (p<0.001) and systemic reactions (p=0.003) (1). Further, a cross-sectional study in 526 PR-10 sensitized individuals in Italy showed that specific Immunoglobulin E (sIgE) reactivity to Pru p 1 was linked with symptoms of OAS (63% of 270) like oral itching, oral mucosa irritation, or angioedema of lips, tongue, or throat. This was significant when compared to respiratory symptoms (53% of 405) (p<0.05) (10). Another study also reported that co-sensitization of Pru p 3, Pru p 1, and/or Pru p 4 among peach allergic patients may provide a shield against severe symptoms due to Pru p 3 (4).
Molecular Aspects
Biochimestry
Pru p 1 belongs to the PR-10 family of pathogenesis-related proteins (12), with Bet v 1 (major birch allergen) being a major member of the family (13) [p299]. The PR-10 proteins are cytosolic proteins having 154-163 amino acids with a molecular weight of 16-18 kDa. They are mostly involved with plant development and defense mechanisms. They have a characteristic hydrophobic core which is the binding site for a variety of ligands (14). Pru p 1 is heat labile and can be easily degraded due to less resistance to enzymatic digestion (1). sdsd
Isoforms, epitopes, antibodies
Pru p 1 has three isoallergens reported to date and its details are provided in the table below (15):
| Isoallergen and variants | Molecular Weight (kDa) | Characteristics |
|---|---|---|
| Pru p 1.0101 | 19.49 |
|
| Pru p 1.0201 | 17.27 |
|
| Pru p 1.0301 | 17.3 |
|
Cross-reactivity
Pru p 1 can cross-react with other PR-10 protein families that are homologous to Bet v 1 protein such as Rosaceae fruits, hazelnut, carrot, and celery (19). Besides, PR-10 proteins are also found in plants of the Fagales order (birch, hazel, beech) and also in distantly related food sources like peach, peanut, strawberry, and cherry (14).
Pru p 1.01 in peach consists of a proline residue in the p-loop which is like the structure in Bet v 1 isoforms (birch pollen) and Mal d 1.01 (apple) (20). IgE cross-reactivity was found to be highest (88%) between Pru p 1 and Mal d 1 (apple) in a cross-sectional study. Thus, showing that a resembling protein structure can also result in cross-reactivity (10). Moreover, Pru p 1 has 59% and 86% identical amino acid sequence with Bet v 1 and Mal d 1 respectively (12).
Further, amino acid sequence homology of Pru p 1 is also observed with other fruits such as cherry (98%), apricot (76%), and pear (83%) (12).
Diagnostic Relevance
Disease Severity
Pru p 1 is a heat-labile protein and thus easily destroyed by cooking (12) making cooked peach tolerable in aspects of allergenicity (19). Thus, only the unprocessed form of the fruit leads to the usual symptoms such as local oropharyngeal symptoms (8) . A study conducted on 27 peach allergic patients has shown that serum specific IgE of Pru p 1 was found to be higher in patients experiencing local symptoms (91.7%) as compared to patients experiencing systemic symptoms including anaphylaxis (80%) (5).
Exposure
The main exposure route for this allergen is through ingestion (15).
Compiled By
Author: Turacoz Healthcare Solutions
Reviewer: Dr. Christian Fischer
Last reviewed: January 2021
References
- Gaier S, Oberhuber C, Hemmer W, Radauer C, Rigby NM, Marsh JT, et al. Pru p 3 as a marker for symptom severity for patients with peach allergy in a birch pollen environment. J Allergy Clin Immunol. 2009;124(1):166-7.
- Boyano-Martinez T, Pedrosa M, Belver T, Quirce S, Garcia-Ara C. Peach allergy in Spanish children: tolerance to the pulp and molecular sensitization profile. Pediatr Allergy Immunol. 2013;24(2):168-72.
- Brusca I, Barrale M, Onida R, La Chiusa SM, Gjomarkaj M, Uasuf CG. The extract, the molecular allergen or both for the in vitro diagnosis of peach and peanut sensitization? Clin Chim Acta. 2019;493:25-30.
- Uasuf CG, Villalta D, Conte ME, Di Sano C, Barrale M, Cantisano V, et al. Different co-sensitizations could determine different risk assessment in peach allergy? Evaluation of an anaphylactic biomarker in Pru p 3 positive patients. Clin Mol Allergy. 2015;13:30.
- Ando Y, Miyamoto M, Kato M, Nakayama M, Fukuda H, Yoshihara S. Pru p 7 Predicts Severe Reactions after Ingestion of Peach in Japanese Children and Adolescents. Int Arch Allergy Immunol. 2020;181(3):183-90.
- Inomata N, Miyakawa M, Aihara M. Eyelid edema as a predictive factor for sensitization to Pru p 7 in peach allergy. J Dermatol. 2016;43(8):900-5.
- Hwang EK, Kim JH, Nam YH, Jin HJ, Park HS. Diagnostic value of the allergen, Pru p 1 in adult patients with birch pollen-associated oral allergy syndrome. Allergy. 2011;66(12):1621-2.
- Ballmer-Weber B, Hoffmann-Sommergruber K. B15. ALLERGY TO FRUITS AND VEGETABLES. In: Matricardi P. M. K-TJ, Hoffmann H. J., et al., editor. MOLECULAR ALLERGOLOGY USER'S GUIDE. Switerland: EAACI; 2016.
- van Ree R, Aalberse CR. A02. ALLERGENS AND THE ALLERGENIC COMPOSITION OF SOURCE MATERIALS. In: Matricardi P. M. K-TJ, Hoffmann H. J., et al., editor. Molecular Allergology User's Guide. Switzerland: The European Academy of Allergy and Clinical Immunology (EAACI); 2016. p. 11-20.
- Scala E, Abeni D, Cecchi L, Guerra EC, Locanto M, Pirrotta L, et al. Molecular Recognition Profiles and Clinical Patterns of PR-10 Sensitization in a Birch-Free Mediterranean Area. Int Arch Allergy Immunol. 2017;173(3):138-46.
- Guhsl EE, Hofstetter G, Lengger N, Hemmer W, Ebner C, Froschl R, et al. IgE, IgG4 and IgA specific to Bet v 1-related food allergens do not predict oral allergy syndrome. Allergy. 2015;70(1):59-66.
- Gaier S, Marsh J, Oberhuber C, Rigby NM, Lovegrove A, Alessandri S, et al. Purification and structural stability of the peach allergens Pru p 1 and Pru p 3. Mol Nutr Food Res. 2008;52 Suppl 2:S220-9.
- Brieteneder H, Kleine-Tebbe J. C02. PR-10 LIKE ALLERGENS. In: Matricardi P. M. K-TJ, Hoffmann H. J., et al., editor. MOLECULAR ALLERGOLOGY USER'S GUIDE. Switerland: EAACI; 2016.
- Aglas L, Soh WT, Kraiem A, Wenger M, Brandstetter H, Ferreira F. Ligand Binding of PR-10 Proteins with a Particular Focus on the Bet v 1 Allergen Family. Curr Allergy Asthma Rep. 2020;20(7):25.
- WHO/IUIS. International Union of Immunological Societies Allergen Nomenclature 2019 [29-Dec-2020]. Available from: http://www.allergen.org/viewallergen.php?aid=557.
- Zubini P, Zambelli B, Musiani F, Ciurli S, Bertolini P, Baraldi E. The RNA Hydrolysis and the Cytokinin Binding Activities of PR-10 Proteins Are Differently Performed by Two Isoforms of the Pru p 1 Peach Major Allergen and Are Possibly Functionally Related. Plant Physiology. 2009;150:1235-47.
- Gao ZS, Zhou X, Yang ZW, Versteeg SA, Gao L, Fu WY, et al. IgE-binding potencies of three peach Pru p 1 isoforms. Mol Nutr Food Res. 2016;60(11):2457-66.
- Yang Z, Ma Y, Chen L, Xie R, Zhang X, Zhang B, et al. Differential transcript abundance and genotypic variation of four putative allergen-encoding gene families in melting peach. Tree Genetics & Genomes. 2011;7:903-16.
- Sastre J. Molecular diagnosis in allergy. Clin Exp Allergy. 2010;40(10):1442-60.
- Chen L, Zhang S, Illa E, Song L, Wu S, Howad W, et al. Genomic characterization of putative allergen genes in peach/almond and their synteny with apple. BMC Genomics. 2008;9:543.
- Kleine-Tebbe J, Ballmer-Weber B, Brieteneder H, Vieths S. Bet v 1 and its homologs: Triggers of Tree-Pollen Allergy and Birch Pollen-Associated Cross-Reactions. In: Kleine-Tebbe J, Jakob T, editors. Molecular Allergy Diagnostics: Innovation for a Better Patient Management: Springer; 2017. p. 21-43.
