Bacteroides Lipopolysaccharides (LPS) Induce Anaphylactoid and Lethal Reactions in LPS-Responsive and -Nonresponsive Mice Primed with Muramyl Dipeptide

Takada, Haruhiko; Hirai, H.; Fujiwara, Taku; Kinoshita, Toshihiko; Ogawa, Tomohiko; Hamada, Shigeyuki

doi:10.1093/infdis/162.2.428

Cited by 57 publications

(51 citation statements)

References 33 publications

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“…TNF production was apparently not essential for induction of anaphylaxis, as the reaction was elicited in C3H=HeJ mice in the absence of detectable TNF production [35]. In the present study, only P. vulgaris O25 LPS induced strong anaphylactoid reactions like those evoked by K. pneumoniae O3 LPS, and little or no TNF or NO production was detected, confirming that TNF and NO do not participate in LPSinduced anaphylaxis.…”

Section: Discussionsupporting

confidence: 69%

Bacterial pathogenicity

Ala’Aldeen¹,

Wooldridge²

2012

Medical Microbiology

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Section: Discussionsupporting

confidence: 69%

Bacterial pathogenicity

Ala’Aldeen¹,

Wooldridge²

2012

Medical Microbiology

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“…It was previously demonstrated that P. gingivalis LPS exhibited weak lethal toxicity (40). To sensitize mice to the lethal effects of LPS preparations, we used D-GalN (10).…”

Section: Methodsmentioning

confidence: 99%

Lipopolysaccharide Preparation Extracted fromPorphyromonas gingivalisLipoprotein-Deficient Mutant Shows a Marked Decrease in Toll-Like Receptor 2-Mediated Signaling

et al. 2005

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We recently demonstrated that a new PG1828-encoded lipoprotein (PG1828LP) was able to be separated from a Porphyromonas gingivalis lipopolysaccharide (LPS) preparation, and we found that it exhibited strong cell activation, similar to that of Escherichia coli LPS, through a Toll-like receptor 2 (TLR2)-dependent pathway. In order to determine the virulence of PG1828LP toward cell activation, we generated a PG1828-deficient mutant of P. gingivalis strain 381 by allelic exchange mutagenesis using an ermF-ermAM antibiotic resistance cassette. A highly purified preparation of LPS from a PG1828-deficient mutant (⌬PG1828-LPS) showed nearly the same ladder-like patterns in silver-stained gels as a preparation of LPS from a wild-type strain (WT-LPS), as well as Limulus amoebocyte lysate activities that were similar to those of the WT-LPS preparation. However, the ability of the ⌬PG1828-LPS preparation to activate NF-B in TLR2-expressing cells was markedly attenuated. Cytokine production by human gingival fibroblasts was also decreased in response to the ⌬PG1828-LPS preparation in comparison with the WT-LPS preparation, and the activity was comparable to the stimulation of highly purified lipid A of P. gingivalis by TLR4. Further, lethal toxicity was rarely observed following intraperitoneal injection of the PG1828-deficient mutant into mice compared to that with the wild-type strain, while the ⌬PG1828-LPS preparation showed no lethal toxicity. Taken together, these results clearly indicate that PG1828LP plays an essential role in inflammatory responses and may be a major virulence factor of P. gingivalis.Porphyromonas gingivalis has been implicated as a major etiological agent in the development and progression of chronic periodontitis, which is a destructive inflammatory disease of the supporting tissues of the teeth (38). This bacterium is a gram-negative, obligate anaerobic, oral black-pigmented rod that possesses a large number of potential virulence factors, such as fimbriae, hemagglutinin, lipopolysaccharide (LPS), and various proteases (15).Among these virulence factors, LPS is well known as a major component of the outer membranes of gram-negative bacteria, and it exhibits powerful immunostimulatory and inflammatory activities (32). However, P. gingivalis LPS has a lower level of endotoxic potency than other types of enterobacterial LPSs (21, 27), while it and its active center, lipid A, have been shown to have other properties, such as an ability to activate cells from LPS-hyporesponsive C3H/HeJ mice as well as those from LPS-responsive C3H/HeN mice (18, 42).Toll-like receptor 4 (TLR4) and its accessory protein MD-2 are known to function as signaling receptors for various LPSs (44), and C3H/HeJ mice have been demonstrated to be hyporesponders, due to a natural point mutation of TLR4 (30). Further, TLR2 has been shown to be an essential signal-transducing molecule for P. gingivalis LPS preparations (4, 13), although P. gingivalis LPS is thought to be associated with quite different lipid A phosphorylation and acy...

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“…wt of 41 000 was isolated from freshly cultivated whole cells of P. gingivalis and puri®ed chromatographically as described previously [25]. LPS was prepared by the hot phenol-water extraction method as described previously [26].…”

Section: Methodsmentioning

confidence: 99%

Enhancement of hepatocyte growth factor (scatter factor) production by human gingival fibroblasts in culture stimulated with Porphyromonas gingivalis fimbriae

Sugiyama

Ogawa

Daikuhara

et al. 2000

Journal of Medical Microbiology

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Hepatocyte growth factor (HGF), also known as scatter factor (SF), is a motogen, mitogen and morphogen produced by mesenchymal cells that mainly acts on epithelial cells and is involved in osteoclast stimulation. This study examined the possible enhanced production of HGF=SF by human gingival ®broblasts upon stimulation with killed cells of Porphyromonas gingivalis strain 381 and its representative bioactive cellular components, ®mbriae and lipopolysaccharide (LPS). P. gingivalis whole cells enhanced the production of HGF=SF detected by ELISA in culture supernates of the ®broblasts. Fimbriae prepared from P. gingivalis exhibited powerful HGF=SF-inducing activity in a concentration-dependent manner, with peak activity observed at 100±200 ìg=ml. The ®mbriae-induced HGF=SF mRNA expression by the cells was also detected by reverse transcription-PCR. P. gingivalis LPS exhibited weak HGF=SF-inducing activity. The study also examined the HGF=SF-inducing activity of seven synthetic peptides corresponding to the segments of P. gingivalis ®mbrial subunit protein. The peptides of residues 282±301 and 302±321, which exhibited antagonistic effects against P. gingivalis ®mbriae-binding to human gingival ®broblasts in a previous study, showed weak activity, whereas other non-antagonistic peptides showed no signi®cant activity. These ®ndings indicated that P. gingivalis ®mbriae enhanced production of HGF=SF by human gingival ®broblasts, whereas synthetic peptide segments of ®mbrial subunit protein were not suf®cient to exert the activity.

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Bacteroides Lipopolysaccharides (LPS) Induce Anaphylactoid and Lethal Reactions in LPS-Responsive and -Nonresponsive Mice Primed with Muramyl Dipeptide

Cited by 57 publications

References 33 publications

Bacterial pathogenicity

Bacterial pathogenicity

Lipopolysaccharide Preparation Extracted fromPorphyromonas gingivalisLipoprotein-Deficient Mutant Shows a Marked Decrease in Toll-Like Receptor 2-Mediated Signaling

Enhancement of hepatocyte growth factor (scatter factor) production by human gingival fibroblasts in culture stimulated with Porphyromonas gingivalis fimbriae

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