Open AccessNon-standard biological activities of lipopolysaccharide from Helicobacter pylori
Author(s) -
Naohiro Matsuyama,
Teruo Kirikae,
Fumiko Kirikae,
Masahito Hashimoto,
Kenichi Amano,
Shunji Hayashi,
Yoshikazu Hirai,
Tatsuya Kubota,
Masayasu Nakano
Publication year - 2001
Publication title -
journal of medical microbiology/journal of medical microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.91
H-Index - 117
eISSN - 1473-5644
pISSN - 0022-2615
DOI - 10.1099/0022-1317-50-10-865
Subject(s) - lipopolysaccharide , polymyxin b , microbiology and biotechnology , lipid a , potency , limulus , helicobacter pylori , polymyxin , tumor necrosis factor alpha , in vitro , chemistry , biology , immunology , antibiotics , biochemistry , paleontology , genetics
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.