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Non-standard biological activities of lipopolysaccharide from Helicobacter pylori

NAOHIRO MATSUYAMA, TERUO KIRIKAE^*, FUMIKO KIRIKAE^*, MASAHITO HASHIMOTO^*, KEN-ICHI AMANO, SHUNJI HAYASHI, YOSHIKAZU HIRAI, TATSUYA KUBOTA and MASAYASU NAKANO

Shiraoka Chuo Sogo Hospital, Shiraoka, Saitama 329-0217, *Department of Infectious Diseases and Tropical Medicine, Research Institute International Medical Center of Japan, Shinjuku, Tokyo 162-8655, Central Research Laboratory, Akita University School of Medicine, Akita 010-8543, Department of Microbiology and Department of Intensive and Critical Care Medicine, Jichi Medical School, minamikawachi-machi, Tochigi 329-0498, Japan

Corresponding author: Dr T. Kirikae (e-mail: tkirikae{at}ri.imcj.go.jp).

Received 15 Jan. 2001; accepted 17 April 2001.

Abstract

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.

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