Novel Strategy To Create Hypoallergenic Peanut Protein–Polyphenol Edible Matrices for Oral Immunotherapy

Abstract

Peanut allergy is an IgE-mediated hypersensitivity. Upon peanut consumption by an allergic individual, epitopes on peanut proteins bind and cross-link peanut-specific IgE on mast cell and basophil surfaces triggering the cells to release inflammatory mediators responsible for allergic reactions. Polyphenolic phytochemicals have high affinity to bind proteins and form soluble and insoluble complexes with unique functionality. This study investigated the allergenicity of polyphenol-fortified peanut matrices prepared by complexing various polyphenol-rich plant juices and extracts with peanut flour. Polyphenol-fortified peanut matrices reduced IgE binding to one or more peanut allergens (Ara h 1, Ara h 2, Ara h 3, and Ara h 6). Attenuated total reflectance-Fourier transform infrared spectroscopy (ATR-FTIR) suggested changes in secondary protein structure. Peanut protein-cranberry polyphenol fortified matrices triggered significantly less basophil degranulation than unmodified flour in an ex vivo assay using human blood and less mast cell degranulation when used to orally challenge peanut-allergic mice. Polyphenol fortification of peanut flour resulted in a hypoallergenic matrix with reduced IgE binding and degranulation capacity, likely due to changes in protein secondary structure or masking of epitopes, suggesting potential applications for oral immunotherapy.

The effect of peanut protein nanoparticles on characteristics of protein- and starch-based nanocomposite films: A comparative study

“…The shifts observed indicated the development of interactions between CS and PNPs functional groups. Amide II around 1535 cm −1 (Plundrich et al, 2014) appeared for CS films with 1, 2, and 4% PNPs, what is more, the increase in the absorption signal could be observed with the increasing of PNPs content. These results evidenced the compatibility of both polymers.…”

Protein-bound polyphenols create “ghost” band artifacts during chemiluminescence-based antigen detection

“…Nitroblue tetrazolium and glycine were purchased from Sigma-Aldrich (Sigma-Aldrich, St. Louis, MO, USA). All other SDS-PAGE and immunoblotting reagents used are listed elsewhere 3 . Egg white protein (EWP) was purchased from Sigma-Aldrich (St. Louis, MO, USA).…”

“…Samples (10 µg protein/10 µL) were incubated for 5 min at 95°C, loaded onto a gel, run (40 min at 200 V), and then stained with Coomassie Brilliant Blue (CBB). The immunoblotting method used, including reagent sources, is described elsewhere 3 . The following minor modifications were made: Pooled human plasma (containing polyclonal antibodies, among them egg white-specific IgE) from 7 egg white-allergic individuals (PlasmaLab International, Everett, WA, USA; 1:80; v/v) was used to bind antigens on the membrane.…”

“…We recently evaluated peanut protein-polyphenol aggregate particles for their binding capacity to peanut-specific plasma IgE from allergic patients using complementary assays, including chemiluminescence-based Western blotting 3 . Previous studies have shown “ghost” bands on some blots.…”

Bioanalytical Methods for Food Allergy Diagnosis, Allergen Detection and New Allergen Discovery

“…Hypoallergenic formulas based on hydrolyzed milk proteins for infants with cow's milk allergy are commercially available since 1985. Recent laboratory studies have shown potential hypoallergenicity of peanut-polyphenol edible matrix [62] and cashew allergens treated with sodium sulfite in a temperature-dependent manner [63].…”