Structure, Stability, and IgE Binding of the Peach Allergen Peamaclein (Pru p 7)

Lisa Tuppo, Roberta Spadaccini, Claudia Alessandri, Hans Wienk, Rolf Boelens, Ivana Giangrieco, Maurizio Tamburrini, Adriano Mari, Delia Picone, Maria Antonietta Ciardiello*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

Abstract

Knowledge of the structural properties of allergenic proteins is a necessary prerequisite to better understand the molecular bases of their action, and also to design targeted structural/functional modifications. Peamaclein is a recently identified 7 kDa peach allergen that has been associated with severe allergic reactions in sensitive subjects. This protein represents the first component of a new allergen family, which has no 3D structure available yet. Here, we report the first experimental data on the 3D-structure of Peamaclein. Almost 75% of the backbone resonances, including two helical stretches in the N-terminal region, and four out of six cysteine pairs have been assigned by 2D-NMR using a natural protein sample. Simulated gastrointestinal digestion experiments have highlighted that Peamaclein is even more resistant to digestion than the peach major allergen Pru p 3. Only the heat-denatured protein becomes sensitive to intestinal proteases. Similar to Pru p 3, Peamaclein keeps its native 3D-structure up to 90 degrees C, but it becomes unfolded at temperatures of 100-120 degrees C. Heat denaturation affects the immunological properties of both peach allergens, which lose at least partially their IgE-binding epitopes. In conclusion, the data collected in this study provide a first set of information on the molecular properties of Peamaclein. Future studies could lead to the possible use of the denatured form of this protein as a vaccine, and of the inclusion of cooked peach in the diet of subjects allergic to Peamaclein. (C) 2014 Wiley Periodicals, Inc.

Original languageEnglish
Pages (from-to)416-425
Number of pages10
JournalBiopolymers
Volume102
Issue number5
DOIs
Publication statusPublished - Sept 2014

Funding

Contract grant sponsor: European Union (Bio-NMR, Project 261863)

Keywords

  • Peamaclein
  • Pru p 7
  • NMR
  • simulated gastrointestinal digestion
  • heat stability
  • allergen
  • IgE binding
  • LIPID TRANSFER PROTEINS
  • NMR-SPECTROSCOPY
  • FOOD
  • EPITOPES
  • PRU-P-3
  • IDENTIFICATION
  • REACTIVITY
  • DIGESTION
  • FEATURES
  • FAMILY

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