Characterization of Vibrio cholerae neuraminidase as an immunomodulator for novel formulation of oral allergy immunotherapy

Clin Immunol. 2018 Jul:192:30-39. doi: 10.1016/j.clim.2018.03.017. Epub 2018 Mar 30.

Abstract

To improve current mucosal allergen immunotherapy Vibrio cholerae neuraminidase (NA) was evaluated as a novel epithelial targeting molecule for functionalization of allergen-loaded, poly(D,L-lactide-co-glycolide) (PLGA) microparticles (MPs) and compared to the previously described epithelial targeting lectins wheat germ agglutinin (WGA) and Aleuria aurantia lectin (AAL). All targeters revealed binding to Caco-2 cells, but only NA had high binding specificity to α-L fucose and monosialoganglioside-1. An increased transepithelial uptake was found for NA-MPs in a M-cell co-culture model. NA and NA-MPs induced high levels of IFN-γ and IL10 in naive mouse splenocytes and CCL20 expression in Caco-2. Repeated oral gavage of NA-MPs resulted in a modulated, allergen-specific immune response. In conclusion, NA has enhanced M-cell specificity compared to the other targeters. NA functionalized MPs induce a Th1 and T-regulatory driven immune response and avoid allergy effector cell activation. Therefore, it is a promising novel, orally applied formula for allergy therapy.

Keywords: AAL; M-cell; Neuraminidase; Oral application; PLGA-microparticles; WGA.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Allergens / immunology
  • Allergens / metabolism
  • Allergens / therapeutic use
  • Animals
  • Bacterial Proteins / immunology*
  • Bacterial Proteins / metabolism
  • Caco-2 Cells
  • Cell Line, Tumor
  • Coculture Techniques
  • Desensitization, Immunologic / methods
  • Humans
  • Hypersensitivity / immunology*
  • Hypersensitivity / therapy
  • Immunologic Factors / immunology*
  • Mice, Inbred BALB C
  • Microspheres
  • Mouth Diseases / immunology*
  • Mouth Diseases / therapy
  • Neuraminidase / immunology*
  • Neuraminidase / metabolism
  • Protein Binding
  • Vibrio cholerae / enzymology

Substances

  • Allergens
  • Bacterial Proteins
  • Immunologic Factors
  • Neuraminidase