Present address: Ascentia Corporation, Redmond, WA, USA.
Porphyromonas gingivalis lipopolysaccharide lipid A heterogeneity: differential activities of tetra- and penta-acylated lipid A structures on E-selectin expression and TLR4 recognition
Article first published online: 13 JAN 2006
Volume 8, Issue 5, pages 857–868, May 2006
How to Cite
Reife, R. A., Coats, S. R., Al-Qutub, M., Dixon, D. M., Braham, P. A., Billharz, R. J., Howald, W. N. and Darveau, R. P. (2006), Porphyromonas gingivalis lipopolysaccharide lipid A heterogeneity: differential activities of tetra- and penta-acylated lipid A structures on E-selectin expression and TLR4 recognition. Cellular Microbiology, 8: 857–868. doi: 10.1111/j.1462-5822.2005.00672.x
- Issue published online: 13 JAN 2006
- Article first published online: 13 JAN 2006
- Received 29 August, 2005; revised 31 October, 2005; accepted 15 November, 2005.
Porphyromonas gingivalis is a Gram-negative bacterium strongly associated with periodontitis, a chronic inflammatory disease of the tissue surrounding the tooth root surface. Lipopolysaccharide (LPS) obtained from P. gingivalis is unusual in that it has been shown to display an unusual amount of lipid A heterogeneity containing both tetra- and penta-acylated lipid A structures. In this report, it is shown that penta-acylated lipid A structures facilitate E-selectin expression whereas tetra-acylated lipid A structures do not. Furthermore, it is shown that tetra-acylated lipid A structures are potent antagonists for E-selectin expression. Both tetra- and penta-acylated lipid A structures interact with TLR4 although experiments utilizing human, mouse and human/mouse chimeric TLR4 proteins demonstrated that they interact differentially with the TLR4 signalling complexes. The presence of two different structural types of lipid A in P. gingivalis LPS, with opposing effects on the E-selectin response suggests that this organism is able to modulate innate host responses by alterations in the relative amount of these lipid A structures.