scholarly journals Differential modulation of human β-defensins expression in human gingival epithelia by Porphyromonas gingivalis lipopolysaccharide with tetra- and penta-acylated lipid A structures

2009 ◽  
Vol 15 (6) ◽  
pp. 325-335 ◽  
Author(s):  
Qian Lu ◽  
Richard P. Darveau ◽  
Lakshman P. Samaranayake ◽  
Cun-Yu Wang ◽  
Lijian Jin
Keyword(s):  
Porphyromonas Gingivalis ◽  
Lipid A ◽  
Differential Modulation ◽  
Porphyromonas Gingivalis Lipopolysaccharide

Biological properties of the native and synthetic lipid A of Porphyromonas gingivalis lipopolysaccharide

2007 ◽  
Vol 23 (1) ◽  
pp. 60-69 ◽  
Author(s):  
H. Kumada ◽  
Y. Haishima ◽  
K. Watanabe ◽  
C. Hasegawa ◽  
T. Tsuchiya ◽  
...  
Keyword(s):  
Porphyromonas Gingivalis ◽  
Lipid A ◽  
Biological Properties ◽  
Porphyromonas Gingivalis Lipopolysaccharide

scholarly journals Free Lipid A Isolated from Porphyromonas gingivalis Lipopolysaccharide Is Contaminated with Phosphorylated Dihydroceramide Lipids: Recovery in Diseased Dental Samples

2011 ◽  
Vol 80 (2) ◽  
pp. 860-874 ◽  
Author(s):  
Frank C. Nichols ◽  
Bekim Bajrami ◽  
Robert B. Clark ◽  
William Housley ◽  
Xudong Yao
Keyword(s):  
Porphyromonas Gingivalis ◽  
Lipid A ◽  
Alveolar Bone ◽  
Ionization Mass ◽  
Subgingival Plaque ◽  
Content Type ◽  
Free Lipid ◽  
The Matrix ◽  
Tlr2 Activation ◽  
Porphyromonas Gingivalis Lipopolysaccharide

ABSTRACTRecent reports indicate thatPorphyromonas gingivalismediates alveolar bone loss or osteoclast modulation through engagement of Toll-like receptor 2 (TLR2), though the factors responsible for TLR2 engagement have yet to be determined. Lipopolysaccharide (LPS) and lipid A, lipoprotein, fimbriae, and phosphorylated dihydroceramides ofP. gingivalishave been reported to activate host cell responses through engagement of TLR2. LPS and lipid A are the most controversial in this regard because conflicting evidence has been reported concerning the capacity ofP. gingivalisLPS or lipid A to engage TLR2 versus TLR4. In the present study, we first preparedP. gingivalisLPS by the Tri-Reagent method and evaluated this isolate for contamination with phosphorylated dihydroceramide lipids. Next, the lipid A prepared from this LPS was evaluated for the presence of phosphorylated dihydroceramide lipids. Finally, we characterized the lipid A by the matrix-assisted laser desorption ionization mass spectrometry (MALDI-MS) and electrospray-MS methods in order to quantify recovery of lipid A in lipid extracts from diseased teeth or subgingival plaque samples. Our results demonstrate that both the LPS and lipid A derived fromP. gingivalisare contaminated with phosphorylated dihydroceramide lipids. Furthermore, the lipid extracts derived from diseased teeth or subgingival plaque do not contain free lipid A constituents ofP. gingivalisbut contain substantial amounts of phosphorylated dihydroceramide lipids. Therefore, the free lipid A ofP. gingivalisis not present in measurable levels at periodontal disease sites. Our results also suggest that the TLR2 activation of host tissues attributed to LPS and lipid A ofP. gingivaliscould actually be mediated by phosphorylated dihydroceramides.

scholarly journals Porphyromonas gingivalis Lipopolysaccharide Contains Multiple Lipid A Species That Functionally Interact with Both Toll-Like Receptors 2 and 4

2004 ◽  
Vol 72 (9) ◽  
pp. 5041-5051 ◽  
Author(s):  
Richard P. Darveau ◽  
Thu-Thao T. Pham ◽  
Kayde Lemley ◽  
Robert A. Reife ◽  
Brian W. Bainbridge ◽  
...  
Keyword(s):  
Bone Marrow ◽  
Porphyromonas Gingivalis ◽  
Cell Activation ◽  
Lipid A ◽  
Bone Marrow Cells ◽  
Biological Significance ◽  
Double Knockout ◽  
Hek 293 ◽  
Porphyromonas Gingivalis Lipopolysaccharide ◽  
Marrow Cells

ABSTRACT The innate host response to lipopolysaccharide (LPS) obtained from Porphyromonas gingivalis is unusual in that different studies have reported that it can be an agonist for Toll-like receptor 2 (TLR2) as well as an antagonist or agonist for TLR4. In this report it is shown that P. gingivalis LPS is highly heterogeneous, containing more lipid A species than previously described. In addition, purification of LPS can preferentially fractionate these lipid A species. It is shown that an LPS preparation enriched for lipid A species at m/z 1,435 and 1,450 activates human and mouse TLR2, TLR2 plus TLR1, and TLR4 in transiently transfected HEK 293 cells coexpressing membrane-associated CD14. The HEK cell experiments further demonstrated that cofactor MD-2 was required for functional engagement of TLR4 but not of TLR2 nor TLR2 plus TLR1. In addition, serum-soluble CD14 effectively transferred P. gingivalis LPS to TLR2 plus TLR1, but poorly to TLR4. Importantly, bone marrow cells obtained from TLR2−/− and TLR4−/− mice also responded to P. gingivalis LPS in a manor consistent with the HEK results, demonstrating that P. gingivalis LPS can utilize both TLR2 and TLR4. No response was observed from bone marrow cells obtained from TLR2 and TLR4 double-knockout mice, demonstrating that P. gingivalis LPS activation occurred exclusively through either TLR2 or TLR4. Although the biological significance of the different lipid A species found in P. gingivalis LPS preparations is not currently understood, it is proposed that the presence of multiple lipid A species contributes to cell activation through both TLR2 and TLR4.

scholarly journals Synthetic tetra-acylated derivatives of lipid A from Porphyromonas gingivalis are antagonists of human TLR4

2008 ◽  
Vol 6 (18) ◽  
pp. 3371 ◽  
Author(s):  
Yanghui Zhang ◽  
Jidnyasa Gaekwad ◽  
Margreet A. Wolfert ◽  
Geert-Jan Boons
Keyword(s):  
Porphyromonas Gingivalis ◽  
Lipid A ◽  
Derivatives Of

Porphyromonas gingivalis Lipopolysaccharide Induces a Pro-inflammatory Human Gingival Fibroblast Phenotype

Inflammation ◽  
2016 ◽  
Vol 40 (1) ◽  
pp. 144-153 ◽  
Author(s):  
S. Buket Bozkurt ◽  
Sema S. Hakki ◽  
Erdogan E. Hakki ◽  
Yusuf Durak ◽  
Alpdogan Kantarci
Keyword(s):  
Porphyromonas Gingivalis ◽  
Human Gingival Fibroblast ◽  
Gingival Fibroblast ◽  
Porphyromonas Gingivalis Lipopolysaccharide
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