Allergy Asthma Immunol Res.  2019 Jan;11(1):143-151. 10.4168/aair.2019.11.1.143.

Pollen/Fruit Syndrome: Clinical Relevance of the Cypress Pollen Allergenic Gibberellin-Regulated Protein

  • 1Department of Biochemistry, Armand Trousseau Children Hospital, APHP, A&E Research Team, Paris, France.
  • 2Paris-Sud Analytical Chemistry Group, Paris-Sud University, Orsay, France.
  • 3Department of Biochemistry, Armand Trousseau Children Hospital, APHP, Paris, France.
  • 4Razi Vaccine and Serum Research Institute, Agricultural Research, Education and Extension Organization, Karaj, Iran.
  • 5Global Institution for Collaborative Research and Education, Protein Science Laboratory, Hokkaïdo University, Sapporo, Japan.
  • 6Beckman Coulter, Life Sciences Research, Marseille, France.
  • 7Department of Allergology, Pasteur Institute Medical Center, Paris, France.
  • 8Department of Pneumonology and Allergy, La Timone Hospital, APHM, Aix-Marseille University, Marseille, France.
  • 9Pasteur Institute, Center of Resources and Technological Research, Paris, France.


A pollen/food-associated syndrome (PFAS) has been described between peach and cypress pollen. Cross-reactive allergens were characterized which belong to the Gibberellin-regulated protein (GRP) family, BP14 in cypress pollen and Pru p 7 in peach. GRP are small cationic protein with anti-microbial properties. A patient suffering from a peach/cypress syndrome was explored clinically and biologically using 2 types of immunoglobulin E (IgE) multiarray microchip, immunoblots and a basophil activation test to assess the clinical relevance of various extracts and purified allergens from fruits or cypress pollen. In addition to PR10 sensitization, the patient showed specific IgE to Pru p 7, BP14 and allergen from pomegranate. These last 3 allergens and allergenic sources are able to induce ex vivo basophil activation characterized by the monitoring of the expression of CD63 and CD203c, both cell surface markers correlated with a basophil mediator release. Up to 100% of cells expressed CD203c at 50 ng/mL of BP14 protein. In contrast, snakin-1, a GRP from potato sharing 82% sequence identity with Pru p 7 did not activate patient's basophils. These results strongly suggest that, like Pru p 7, BP14 is a clinically relevant allergenic GRP from pollen. Allergen members of this newly described protein family are good candidates for PFAS where no cross-reactive allergens have been characterized.


Cypress; pollen; peach; pomegranate; allergen; basophil

MeSH Terms

Immunoglobulin E
Prunus persica
Solanum tuberosum
Immunoglobulin E


  • Fig. 1 IgE immunoreactivity to extracts and proteins. (A) SDS-PAGE coomassie blue (lanes 5, 7, 8) or silver nitrate (lanes 1, 2, 3, 4, 6, 9, 10) stained proteins. IgE immunoblots with patient serum (lanes 0 to 10). Negative controls (B) 2-DE. Left panel: silver-stained total proteins. Right panel: IgE immunoblot with patient serum. Relative molecular masses in kDa. SDS-PAGE, sodium dodecyl sulfate polyacrylamide gel electrophoresis; 2-DE, two-dimensional gel electrophoresis.

  • Fig. 2 Basophil activation test: ex vivo activation of patient's basophils expressing CD203c (A) or CD63 (B) standardized activation markers (anti-IgE, 100% activation), (no allergen, 0% activation). Four serial concentrations were used: 10 to 104 ng/mL of each extract, 1 to 103 ng/mL for recombinant proteins and 5 to 5 × 103 ng/mL for native BP14. One concentration of each allergenic source was used for the control patient's basophils.


1. Kim MA, Kim DK, Yang HJ, Yoo YY, Park HS, et al. Pollen-Food allergy syndrome in Korean pollinosis patients: a nationwide survey. Allergy Asthma Immunol Res. 2018.
2. Werfel T, Asero R, Ballmer-Weber BK, Beyer K, Enrique E, Knulst AC, et al. Position paper of the EAACI: food allergy due to immunological cross-reactions with common inhalant allergens. Allergy. 2015; 70:1079–1090.
3. Hugues B, Didierlaurent A, Charpin D. Cross-reactivity between cypress pollen and peach: a report of seven cases. Allergy. 2006; 61:1241–1243.
4. Sénéchal H, Šantrůček J, Melčová M, Svoboda P, Zídková J, Charpin D, et al. A new allergen family involved in pollen food-associated syndrome: Snakin/gibberellin-regulated proteins. J Allergy Clin Immunol. 2018; 141:411–414.e4.
5. Nahirñak V, Almasia NI, Hopp HE, Vazquez-Rovere C. Snakin/GASA proteins: involvement in hormone crosstalk and redox homeostasis. Plant Signal Behav. 2012; 7:1004–1008.
6. Kuddus MR, Rumi F, Tsutsumi M, Takahashi R, Yamano M, Kamiya M, et al. Expression, purification and characterization of the recombinant cysteine-rich antimicrobial peptide snakin-1 in Pichia pastoris. Protein Expr Purif. 2016; 122:15–22.
7. Shahali Y, Sutra JP, Haddad I, Vinh J, Guilloux L, Peltre G, et al. Proteomics of cypress pollen allergens using double and triple one-dimensional electrophoresis. Electrophoresis. 2012; 33:462–469.
8. Shahali Y, Sutra JP, Hilger C, Swiontek K, Haddad I, Vinh J, et al. Identification of a polygalacturonase (Cup s 2) as the major CCD-bearing allergen in Cupressus sempervirens pollen. Allergy. 2017; 72:1806–1810.
9. Senechal H, Charpin D, Couderc R, Poncet P. Gibberellin-regulated proteins and the enigma of the “missing link”. Rev Fr Allergol. 2018; 58:63–67.
10. Tuppo L, Alessandri C, Pasquariello MS, Petriccione M, Giangrieco I, Tamburrini M, et al. Pomegranate cultivars: identification of the new IgE-binding protein pommaclein and analysis of antioxidant variability. J Agric Food Chem. 2017; 65:2702–2710.
11. Tuppo L, Alessandri C, Pomponi D, Picone D, Tamburrini M, Ferrara R, et al. Peamaclein--a new peach allergenic protein: similarities, differences and misleading features compared to Pru p 3. Clin Exp Allergy. 2013; 43:128–140.
Full Text Links
  • AAIR
export Copy
  • Twitter
  • Facebook
Similar articles
Copyright © 2023 by Korean Association of Medical Journal Editors. All rights reserved.     E-mail: