Pomegranate chitinase III: Identification of a new allergen and analysis of sensitization patterns to chitinases

Publication date: November 2018

Source: Molecular Immunology, Volume 103

Author(s): Lisa Tuppo, Ivana Giangrieco, Claudia Alessandri, Teresa Ricciardi, Chiara Rafaiani, Michela Ciancamerla, Rosetta Ferrara, Danila Zennaro, Maria Livia Bernardi, Maurizio Tamburrini, Adriano Mari, Maria Antonietta Ciardiello

Abstract

Allergy to pomegranate is often associated with severe symptoms. Two allergens have previously been described: 9k-LTP Pun g 1 and pommaclein Pun g 7. This study describes the isolation of a chitinase III, identified by direct protein sequencing and mass spectrometry. It is a 29-kDa protein showing 69% sequence identity with the latex hevamine and IgE binding in dot blotting, immunoblotting and FABER^®test. Chitinase-specific IgE were detected in 69 of 357 patients sensitized to one or more pomegranate allergenic preparations present on the FABER^®test. Using this test, 19.2% of the patients sensitized to kiwifruit chitinase IV were also sensitized to pomegranate chitinase III, rather than to latex chitinase I (7.2%) with which it shares the N-terminal hevein-like domain. In conclusion, a new allergen has been identified, contributing to improving food allergy diagnosis. This study reveals the important role of chitinases III and IV as allergy sensitizers and prompts further investigations.

Graphical abstract

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