Glycosylation reduces the allergenicity of turbot (Scophthalmus maximus) parvalbumin by regulating digestibility, cellular mediators release and Th1/Th2 immunobalance

Food Chem. 2022 Jul 15:382:132574. doi: 10.1016/j.foodchem.2022.132574. Epub 2022 Feb 25.

Abstract

With turbot being increasingly consumed, turbot parvalbumin (TPV) allergy has become a pressing problem requiring immediate resolution. Glycosylation treatment not only resulted in cross-link formation but also caused changes in the simulated gastric fluid and simulated intestinal fluid digestion stability of TPV. In addition, KU812 experimentation revealed lower levels of β-hexosaminidase, histamine, tryptase, interleukin 4 (IL-4)/IL-13 in glycated protein-treated mice compared with native PV-treated ones. Glycated TPV exhibited a weaker allergic reaction compared with native TPV. Systemic anaphylaxis resulted in mild anaphylactic responses and reduced temperature, along with significantly increased levels of immunoglobulin E and histamine. Furthermore, glycosylation treatment reduced the release of cellular mediators and cytokines (IL-4/IL-13). Glycation to T-PV decreased allergic responses by downregulating Th2 cytokines, regulated the Th1/Th2 balance and effectively reduce the allergenicity and sensitisation ability of T-PV.

Keywords: Allergenicity; Cellular mediators; Glycosylation modification; In vitro digestibility; Th1/Th2 immunobalance; Turbot parvalbumin.

MeSH terms

  • Allergens
  • Anaphylaxis*
  • Animals
  • Cytokines
  • Flatfishes*
  • Glycosylation
  • Mice
  • Mice, Inbred BALB C
  • Parvalbumins / genetics
  • Th1 Cells
  • Th2 Cells

Substances

  • Allergens
  • Cytokines
  • Parvalbumins