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Biological activities of lipopolysaccharides of Proteus spp. and their interactions with polymyxin B and an 18-kDa cationic antimicrobial protein (CAP18)-derived peptide

ANNA ST SWIERZKO, TERUO KIRIKAE^*,, FUMIKO KIRIKAE^*,, MICHIMASA HIRATA, MACIEJ CEDZYNSKI, ANDRZEJ ZIOLKOWSKI, YOSIKAZU HIRAI^*, SHOICHI KUSUMOTO, TAKASHI YOKOCHI^|| and MASAYASU NAKANO^*

Microbiology and Virology Centre, Polish Academy of Science, Lodz 93-232, Poland, *Department of Microbiology, Jichi Medical School, Minamikawachi-machi, Tochigi-ken 329-0498, Department of Infectious Diseases and Tropical Medicine, Research Institute, International Medical Center of Japan, Tokyo 162-8655, Department of Bacteriology, School of Medicine, Iwate Medical University, Morioka 020-8505, Faculty of Science, Osaka University, Toyonaka, Osaka 560-0043 and || Department of Microbiology and Immunology, Aichi Medical University, Nagakute, Aichi 480-1195, Japan

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

Received 25 May 1999; accepted 22 July 1999.

Abstract

The saccharide constituents of lipopolysaccharides (LPS) of Proteus spp. vary with the strain and contain unique components about which little is known. The biological activities of LPS and lipid A from S- and R-forms of 10 Proteus strains were examined. LPS from all S-form Proteus strains was lethal to d-(+)-galactosamine (GalN)-loaded, LPS-responsive, C3H/HeN mice, but not to LPS-hypo-responsive C3H/HeJ mice. P. vulgaris O25 LPS evoked strong anaphylactoid reactions in N-acetylmuramyl-l-alanyl-d-isoglutamine (MDP)-primed C3H/HeJ mice. LPS from S- and R-form Proteus strains induced production of nitric oxide (NO) and tumour necrosis factor (TNF) by macrophages isolated from C3H/HeN but not C3H/HeJ mice. Lipid A from Proteus strains also induced NO and TNF production, although lipid A was less potent than LPS. The effects of LPS were mainly dependent on CD14; LPS-induced NO and TNF production in CD14⁺ J774.1 cells was significantly greater than in CD14^- J7.DEF.3 cells. All LPS from Proteus strains, and especially from P. vulgaris O25, exhibited higher anti-complementary activity than LPS from Escherichia coli or Pseudomonas aeruginosa. Polymyxin B inactivated proteus LPS in a dose-dependent manner, but these LPS preparations were more resistant to polymyxin B than E. coli LPS. CAP18_109--135 , a granulocyte-derived peptide, inhibited proteus LPS endotoxicity only when the LPS:CAP18_109--135 ratio was appropriate, which suggests that CAP18_109--135 acts through a different mechanism than polymyxin B. The results indicate that LPS from Proteus spp. are potently endotoxic, but that the toxicity is different from that of LPS from E. coli or Salmonella spp. and even varies among different Proteus strains. The variation in biological activities among proteus LPS may be due to unique components within the respective LPS.

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