The polysaccharide portion plays an indispensable role in Salmonella lipopolysaccharide-induced activation of NF-kappaB through human toll-like receptor 4

Infect Immun. 2002 Nov;70(11):6043-7. doi: 10.1128/IAI.70.11.6043-6047.2002.

Abstract

The lipid A portion has been identified as the active center responsible for lipopolysaccharide (LPS)-induced macrophage activation. However, we found that Salmonella (Salmonella enterica serovars Abortusequi, Minnesota, and Typhimurium) lipid A is inactive in human macrophages, despite its LPS being highly active. Thus we investigated the critical role of polysaccharide in Salmonella LPS-induced activation of NF-kappaB. In human monocytic cell line THP-1, Salmonella lipid A and synthetic Salmonella-type lipid A (516) did not induce NF-kappaB-dependent reporter activity up to 1 micro g/ml, whereas strong activation was observed in response to Salmonella LPS. The difference in activity between this lipid A and LPS was further examined by using 293 cells expressing human CD14/Toll-like receptor 4 (TLR4)/MD-2, and similar results were obtained in these cells as well. A polysaccharide preparation obtained from Salmonella LPS was inactive in 293 cells expressing human CD14/TLR4/MD-2 even in combination with 516. Salmonella enterica serovar Minnesota Re LPS, whose structure consists of lipid A and two molecules of 2-keto-3-deoxyoctonic acid, but not its lipid A exhibited strong activity in THP-1 cells and 293 cells expressing human CD14/TLR4/MD-2. These results indicate that the polysaccharide portion covalently bound to lipid A plays the principal role in Salmonella LPS-induced activation of NF-kappaB through human CD14/TLR4/MD-2.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Antigens, Surface / physiology
  • Cell Line
  • Drosophila Proteins*
  • Humans
  • Lipid A / chemistry
  • Lipid A / pharmacology*
  • Lipopolysaccharide Receptors / physiology
  • Lipopolysaccharides / chemistry
  • Lipopolysaccharides / pharmacology*
  • Lymphocyte Antigen 96
  • Membrane Glycoproteins / physiology*
  • Mice
  • NF-kappa B / metabolism*
  • Polysaccharides, Bacterial / pharmacology*
  • Receptors, Cell Surface / physiology*
  • Salmonella / pathogenicity*
  • Toll-Like Receptor 4
  • Toll-Like Receptors

Substances

  • Antigens, Surface
  • Drosophila Proteins
  • LY96 protein, human
  • Lipid A
  • Lipopolysaccharide Receptors
  • Lipopolysaccharides
  • Lymphocyte Antigen 96
  • Membrane Glycoproteins
  • NF-kappa B
  • Polysaccharides, Bacterial
  • Receptors, Cell Surface
  • TLR4 protein, human
  • Toll-Like Receptor 4
  • Toll-Like Receptors