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Capnocytophaga canimorsus  is a usual member of dog's mouths flora that causes rare but dramatic human infections after dog bites. We determined the structure of  C. canimorsus  lipid A. The main features are that it is penta-acylated and composed of a “hybrid backbone” lacking the 4′ phosphate and having a 1 phosphoethanolamine ( P -Etn) at 2-amino-2-deoxy- d -glucose (GlcN).  C. canimorsus  LPS was 100 fold less endotoxic than  Escherichia coli  LPS. Surprisingly,  C. canimorsus  lipid A was 20,000 fold less endotoxic than the  C. canimorsus  lipid A-core. This represents the first example in which the core-oligosaccharide dramatically increases endotoxicity of a low endotoxic lipid A. The binding to human myeloid differentiation factor 2 (MD-2) was dramatically increased upon presence of the LPS core on the lipid A, explaining the difference in endotoxicity. Interaction of MD-2, cluster of differentiation antigen 14 (CD14) or LPS-binding protein (LBP) with the negative charge in the 3-deoxy- d - manno -oct-2-ulosonic acid (Kdo) of the core might be needed to form the MD-2 – lipid A complex in case the 4′ phosphate is not present.

The Lipopolysaccharide from Capnocytophaga canimorsus Reveals an Unexpected Role of the Core-Oligosaccharide in MD-2 Binding