The IgE/IgG binding capacity and structural changes of Alaska Pollock parvalbumin glycated with different reducing sugars

Abstract

Parvalbumin (PV) is one of the major allergens in fish. The aim of our present work was to research the influence mechanism of glycation with different reducing sugars (glucose, fructose, ribose, lactose, and galactose) on the immunoglobulin E (IgE) and immunoglobulin G (IgG) binding capacity and structure changes of PV in Alaska Pollock. PV glycated with glucose or fructose (PV-Glu/ PV-Fru) exhibited the higher IgE/IgG binding capacities than that of ribose, galactose, or lactose. During glycation, the lysine (Lyr), tyrosine (Tyr), and phenylalanine (Phe) of PV were gradually embed into core area of three-dimensional structure of protein, which reflected in the ultraviolet (UV) spectrum and fluorescence spectra. Moreover, the increase of surface hydrophobicity had confirmed the conformation alteration of glycated PV. These results suggest that there is a specific association among the change of PV in glycation and in potential allergenicity. The types and conformation of reducing sugar greatly influenced the IgE/IgG binding capacity of PV, and glycation with ribose and galactose was a promising approach for reducing the IgE/IgG binding capacity of PV from Alaska Pollock. Practical applications Parvalbumin (PV), the major allergen of fish, it can not only maintain the physiological activity of cells, but also cross react with human amyloid protein to alleviate Alzheimer's disease and Parkinson's syndrome. This study revealed that the IgE/IgG binding capacity and structural changes of PV from Alaska Pollock modified by glycation with different reducing sugars. This will help us to understand the sensitization and structural change of the glycated products after the reaction of PV with different reducing sugars. It provides an effective carbonyl source for the preparation of low antigenicity PV based on glycation and lays a foundation for glycation modification of other food allergens.

Maillard Reaction Induced Changes in Allergenicity of Food

“…Zhao et al [ 95 ] found that MR with glucose can reduce the IgE reactivity of recombinant silver carp parvalbumin, because glycation sites overlapped with K88, K97, and K108 in epitopes. Zhang et al [ 96 ] glycated Alaska Pollock parvalbumin with glucose, fructose, ribose, lactose, and galactose, while only the reaction with ribose/galactose reduced its IgE binding capacity. Yang et al [ 97 ] processed parvalbumin by boiling, ultrasonic treatment, ultraviolet treatment, pressure treatment, and MR.…”

Phosphorylation of ovalbumin after pulsed electric fields pretreatment: Effects on conformation and immunoglobulin G/immunoglobulin E-binding ability

“…Also, a large number of hydrophobic groups had been exposed due to proteins unfolding (18). The increase of surface hydrophobicity resulted in the harder binding of IgG or IgE with protein (31). The partial unfolding of OVA induced by phosphorylation may result in the damage of conformational IgG and IgE epitopes and lead to the reduction of IgG and IgE-binding of OVA.…”

Effect of the structure and potential allergenicity of glycated tropomyosin, the shrimp allergen

“…Initially, shrimp TM solution was adjusted to 10 mg mL −1 by phosphate buffer solution (PBS, pH 7.4). According to the previous studies, ribose solutions were prepared at a concentration of 5, 50, 250, 500, 1000, 2000 and 4000 mmol L −1 using the same phosphate buffer during the experiment, respectively (Fu et al ., 2019; Zhang et al ., 2021). The TM and ribose solutions were mixed in equal volumes for 24 h at 60 ℃.…”