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Review
. 2010 Oct;54(1):53-70.
doi: 10.1111/j.1600-0757.2009.00333.x.

Contribution of Porphyromonas gingivalis lipopolysaccharide to periodontitis

Sumita Jain, Richard P Darveau
Review

Contribution of Porphyromonas gingivalis lipopolysaccharide to periodontitis

Sumita Jain et al. Periodontol 2000. 2010 Oct.
No abstract available

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Figures

Figure 1
Figure 1
(a) Schematic of the outer membrane of gram-negative bacteria. Lipopolysaccharide (LPS) forms the outer leaflet of the outer membrane. It is composed of three domains namely the lipid A anchor (red), the core oligosaccharide and the outer-most O-antigen (green), which is variable in structure and immunogenic. (b) Schematic of the prototypical E. coli lipid A structure, whose molecular mass is m/z 1797. Two glucosamine residues are linked by a β-1′,6 linkage. The enzymes LpxA and LpxD add four primary acyl chains (red and blue respectively) to the C2, C3, C2′ and C3′ positions, while MsbB (green) and HtrB (purple) add secondary acyl chains to the primary chains.
Figure 2
Figure 2
Heterogeneity in P. gingivalis lipid A structures. The four main groups of lipid A structures that have been isolated from P. gingivalis under different environmental conditions are depicted. The m/z 1768 structure undergoes dephosphorylation and/or deacylation to give rise to the m/z 1688, m/z 1448 and m/z 1368 lipid A structures. The m/z 1688 structure can also have the phosphate group at the C1 position. Removal of the acyl chain from the C3 position of the m/z 1688 structure gives rise to an m/z 1435 structure (not shown). The acyl chains in red are added by the enzyme LpxD, the chains in blue by LpxA and the secondary acyl chain in purple by HtrB. P. gingivalis lacks a msbB homolog.
Figure 3
Figure 3
MALDI-TOF MS analysis of P. gingivalis lipid A isolated from the wild-type (A-D) when grown in either low (WT lo) or high (WT hi) hemin conditions, and of lipid A isolated from mutants that lack either the C4′-phosphatase PGN_0524 (E, F) or the C1-phosphatase PGN_1713 (G, H) or both (I, J). The column on the left shows the MALDI-TOF MS profile in negative mode, which display negatively charged ions, while those on the right are of the same samples in positive mode, which display uncharged or positively charged ions. Molecular weight (m/z) of ions is plotted on the x-axis and relative intensity of ions on the y-axis. Adapted from (20).
Figure 4
Figure 4
Model of differential 1- and 4′-phosphatase activities, encoded by PGN_1713 and PGN_0524 respectively, under low (left) or high (right) hemin conditions lead to the accumulation of lipid A species that either evade or antagonize innate immune responses. It is proposed that the activity of the lipid A 1-phosphatase, PGN_1713, is inhibited under high hemin conditions. It is also proposed that penta-acylated lipid A species, while being detected by MALDI-TOF MS and thin layer chromatography, are functionally dominated by the inert (low hemin) or antagonistic (high hemin) tetra-acylated lipid A species that are present in wild-type P. gingivalis grown in low and high hemin conditions respectively. Adapted from (20).
See this image and copyright information in PMC

References

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