Non-standard biological activities of lipopolysaccharide from Helicobacter pylori

J Med Microbiol. 2001 Oct;50(10):865-869. doi: 10.1099/0022-1317-50-10-865.


As assessed by the lipopolysaccharide (LPS)-specific chromogenic Limulus amoebocyte lysate (LAL) assay, Helicobacter pylori LPS extracted by the phenol-water procedure showed full potency to coagulate LAL, as did LPS from Salmonella minnesota and Escherichia coli. However, pretreatment of H. pylori LPS with polymyxin B, which easily destroys the endotoxic activity of enterobacterial LPS/lipid A, had little effect on the LAL coagulation activity, although the same treatment of E. coli LPS markedly diminished its activity. The H. pylori LPS induced very weak production of nitric oxide (NO) or tumour necrosis factor (TNF) by murine macrophages and TNF by human peripheral whole blood in vitro in comparison with S. minnesota LPS. These findings indicate that H. pylori LPS has the unique endotoxic characteristic of retaining full LAL coagulation activity with polymyxin B resistance, despite losing its endotoxic potencies such as the ability to induce NO and TNF production.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adult
  • Animals
  • Cells, Cultured
  • Female
  • Helicobacter Infections / microbiology
  • Helicobacter pylori / chemistry
  • Helicobacter pylori / isolation & purification
  • Helicobacter pylori / metabolism*
  • Humans
  • Limulus Test
  • Lipopolysaccharides / isolation & purification
  • Lipopolysaccharides / pharmacology*
  • Lipopolysaccharides / toxicity
  • Macrophages, Peritoneal / drug effects
  • Macrophages, Peritoneal / metabolism
  • Male
  • Mice
  • Mice, Inbred C3H
  • Nitric Oxide / analysis
  • Nitric Oxide / biosynthesis
  • Polymyxin B / pharmacology
  • Tumor Necrosis Factor-alpha / analysis
  • Tumor Necrosis Factor-alpha / biosynthesis


  • Lipopolysaccharides
  • Tumor Necrosis Factor-alpha
  • Nitric Oxide
  • Polymyxin B