Changes in Allergenicity of Ovalbumin in Vitro and in Vivo on Conjugation with Quercetin

J Agric Food Chem. 2020 Apr 1;68(13):4027-4035. doi: 10.1021/acs.jafc.0c00461. Epub 2020 Mar 20.


A previous study demonstrated decreased allergenicity in vitro of some food allergens after conjugation with polyphenols. However, little is known about how polyphenol conjugation with food allergens affects in vivo allergenicity. We conjugated a well-known food allergen, ovalbumin (OVA), with quercetin (QUE) to assess the potential allergenicity of OVA in vitro and in vivo in a BALB/c mouse model. QUE could covalently conjugate with OVA and changed the protein structure, which might destroy and/or mask OVA epitopes. Conjugation with QUE decreased IgE binding properties and the release capacity of the conjugated OVA. In vivo, as compared with native protein, conjugation with QUE decreased the levels of IgE, IgG1, IgG, plasma histamine, and mast cell protease-1 (mMCP-1) on the surface of sensitized mast cells, along with decreased FcεRI+ and c-kit+ expression. The levels of Th2-related cytokines (IL-4, IL-5, IL-13) decreased and that of a Th1-related cytokine (IFN-γ) increased slightly, which suggests that conjugation with QUE modulated the imbalance of the Th1/Th2 immune response. Conjugation of OVA with QUE could reduce OVA allergenicity in vitro and in vivo, which could provide information for reducing food allergenicity by conjugation with polyphenols.

Keywords: OVA; allergenicity; conjugation; mouse model; quercetin.

MeSH terms

  • Allergens / chemistry
  • Allergens / immunology*
  • Animals
  • Cytokines / immunology
  • Food Hypersensitivity / immunology*
  • Humans
  • Immunoglobulin E / immunology
  • Mice
  • Mice, Inbred BALB C
  • Ovalbumin / chemistry
  • Ovalbumin / immunology*
  • Protein Conformation
  • Quercetin / chemistry*
  • Th1 Cells / immunology
  • Th2 Cells / immunology


  • Allergens
  • Cytokines
  • Immunoglobulin E
  • Ovalbumin
  • Quercetin