Purification and Characterization of Pathogenesis Related Class 10 Panallergens

Soheila J Maleki,Barry K Hurlburt,Jane K Mcbride,Hsiaopo Cheng

doi:10.3390/foods8120609

Soheila J Maleki, Barry K Hurlburt + Show 2 more

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https://doi.org/10.3390/foods8120609

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Abstract

Oral allergy syndrome (OAS) describes an allergic reaction where an individual sensitized by pollen allergens develops symptoms after eating certain foods. OAS is caused by cross-reactivity among a class of proteins ubiquitous in plants called pathogenesis related class 10 (PR-10) proteins. The best characterized PR-10 protein is Bet v 1 from birch pollen and its putative function is binding hydrophobic ligands. We cloned a subset of seven recombinant PR-10 proteins from pollens, peanuts, and hazelnuts and developed a standard purification method for them. Immunoglobulin E (IgE) binding of purified PR-10 proteins was analyzed by ImmunoCAP ISAC microarray and enzyme-linked immunosorbent assays (ELISAs) with sera from allergic patients. We investigated the binding activities of PR10s by testing 16 different ligands with each protein and compared their secondary structures using circular dichroism (CD). The PR-10s in this study had very similar CD spectra, but bound IgE with very different affinities. All seven proteins showed a similar pattern of binding to the polyphenol ligands (resveratrol, flavonoids, and isoflavones) and variable binding to other potential ligands (fatty acids, sterols, and plant hormones). We suggest our protocol has the potential to be a near-universal method for PR-10 purification that will facilitate further research into this important class of panallergens.

Highlights

Oral allergy syndrome (OAS) is a condition wherein an individual who has been sensitized to tree or weed pollen develops an Immunoglobulin E (IgE)-mediated reaction upon eating certain fresh fruits or other foods
OAS is mainly caused by the immunological cross-reactivity between pollen allergens belonging to the ubiquitous pathogenesis-related protein-10 (PR-10) family and their homologs in plant foods, notably members of the Rosacae family, celery, legumes, and tree nuts [2,3,4,5,6,7]
This study aims to compare the requirements for purification, secondary structures, and binding to human IgE and potential biological ligands of a subset of recombinant pathogenesis related class 10 (PR-10) proteins

Summary

Introduction

Oral allergy syndrome (OAS) is a condition wherein an individual who has been sensitized to tree or weed pollen develops an Immunoglobulin E (IgE)-mediated reaction upon eating certain fresh fruits or other foods. OAS is mainly caused by the immunological cross-reactivity between pollen allergens belonging to the ubiquitous pathogenesis-related protein-10. The best-characterized member of this protein family is Bet v 1 from Betula verrucosa (white birch) pollen, which is a major cause of seasonal allergies in Central Europe and North America [8]. As most plant PR-10 proteins are labile in structure and readily susceptible to inactivation of their IgE binding ability through heat, processing, or pepsin digestion [4,11], they generally only

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