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• W2035337730 abstract "Signal transduction following binding of lipopolysaccharide (LPS) to Toll-like receptor 4 (TLR4) is an essential aspect of host innate immune responses to infection by Gram-negative pathogens. Here, we describe a novel molecular mechanism used by a prevalent human bacterial pathogen to evade and subvert the human innate immune system. We show that the oral pathogen, Porphyromonas gingivalis, uses endogenous lipid A 1- and 4'-phosphatase activities to modify its LPS, creating immunologically silent, non-phosphorylated lipid A. This unique lipid A provides a highly effective mechanism employed by this bacterium to evade TLR4 sensing and to resist killing by cationic antimicrobial peptides. In addition, lipid A 1-phosphatase activity is suppressed by haemin, an important nutrient in the oral cavity. Specifically, P. gingivalis grown in the presence of high haemin produces lipid A that acts as a potent TLR4 antagonist. These results suggest that haemin-dependent regulation of lipid A 1-dephosphorylation can shift P. gingivalis lipid A activity from TLR4 evasive to TLR4 suppressive, potentially altering critical interactions between this bacterium, the local microbial community and the host innate immune system." @default.
• W2035337730 created "2016-06-24" @default.
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• W2035337730 date "2009-11-01" @default.
• W2035337730 modified "2023-10-03" @default.
• W2035337730 title "Human Toll-like receptor 4 responses to<i>P. gingivalis</i>are regulated by lipid A 1- and 4′-phosphatase activities" @default.
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• W2035337730 doi "https://doi.org/10.1111/j.1462-5822.2009.01349.x" @default.
• W2035337730 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3074576" @default.
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