Lipopolysaccharide ofBurkholderia cepaciaand Its Unique Character To Stimulate Murine Macrophages with Relative Lack of Interleukin-1β-Inducing Ability

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Abstract
Lipopolysaccharide (LPS) ofBurkholderia cepaciawas purified by the conventional phenol-water extraction method (preparation BcLPS-1), followed by enzymatic treatments with DNase, RNase, trypsin, and proteinase K (preparation BcLPS-2), and finally by deoxycholate-phenol-water extraction (preparation BcLPS-3). Cells of LPS-hyporesponsive C3H/HeJ mice were activated by both the BcLPS-1 and the BcLPS-2 preparations but barely activated by BcLPS-3. When LPS-responsive C3H/HeN mice were used as targets, endotoxic activities such as lethal toxicity to galactosamine-sensitized mice, mitogenicity to spleen cells, and activation of macrophages to induce tumor necrosis factor alpha and interleukin-6 (IL-6) were strongly exhibited even by highly purified BcLPS-3 at levels comparable to those of the highly active enterobacterial LPS ofSalmonella entericaserovar Abortus-equi (SaeLPS), used as the control. The ability of BcLPS-3 to activate murine macrophages for induction of IL-1β was, however, much weaker than that of SaeLPS. Both accumulation of pro-IL-1β protein and expression of IL-1β mRNA in macrophages by stimulation with BcLPS-3 were much weaker than by stimulation with SaeLPS. These results indicate that LPS ofB. cepaciahas the potential to play a role as a pathogenic factor with strong activity comparable to that of usual enterobacterial LPS, but unlike the latter, this LPS has a relative lack of ability in the activation of murine macrophages to induce IL-1β. The lack of IL-1β-inducing ability appears to be caused by incomplete signal transduction somewhere in the upstream step(s) of IL-1β gene transcription.