A GalNAc/Gal-specific lectin modulates immune responses via toll-like receptor 4 independently of carbohydrate-binding ability

Chem Commun (Camb). 2021 Jun 22;57(50):6209-6212. doi: 10.1039/d1cc01834e.

Abstract

Toll-like receptor 4 (TLR4) recognizes various protein ligands; however, the protein-TLR4 binding model is unclear. Here we demonstrate a Crenomytilus grayanus lectin (CGL)-TLR4/MD2 model to show that CGL interacts with a TLR4/myeloid differentiation factor 2 (MD2) complex independently of sugar-binding properties. CGL could suppress lipopolysaccharide-induced immune responses significantly, suggesting that TLR4 itself has potential as a therapeutic target.

MeSH terms

  • Animals
  • Binding Sites
  • Bivalvia
  • Carbohydrates / chemistry*
  • Carbohydrates / immunology
  • Humans
  • Lectins / chemistry*
  • Lectins / immunology
  • Lymphocyte Antigen 96 / chemistry*
  • Lymphocyte Antigen 96 / immunology
  • Toll-Like Receptor 4 / chemistry*
  • Toll-Like Receptor 4 / immunology

Substances

  • Carbohydrates
  • LY96 protein, human
  • Lectins
  • Lymphocyte Antigen 96
  • TLR4 protein, human
  • Toll-Like Receptor 4