Properties of oral asaccharolytic black-pigmented <i>Bacteroides</i>

Mayrand, D.; Bourgeau, G.; Grenier, Daniel; Lacroix, Jean-Michel

doi:10.1139/m84-177

Cited by 110 publications

(131 citation statements)

References 8 publications

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“…One bacterium that has attracted considerable interest is Porphyromonas gingivalis as the recovery of this micro-organism from adult periodontitis lesions can be up to 50% of the subgingival anaerobically cultivable flora (Christersson et al, 1989 ;Slots, 1982), whereas it is rarely recovered, and then in low numbers, from healthy sites (Moore et al, 1991). A proportional increase in the level of P. gingivalis in subgingival plaque has been associated with an increased severity of periodontitis (Mayrand & Holt, 1988 ; Socransky et al., 1991) and eradication of the microorganism from the cultivable subgingival microbial population is accompanied by resolution of the disease (Loesche et al, 1981;Van Dyke et al, 1988). Holt et al (1988) have demonstrated the progression of periodontitis lesions in non-human primates with the subgingival implantation of P. gingivalis.…”

Section: Introductionmentioning

confidence: 99%

“…In particular, proteases have received a great deal of attention for their ability to degrade a broad range of host proteins including structural proteins and others involved in defence. The proteins that have been shown to be substrates for P. gingivalis proteolytic activity include collagen types I and IV, fibronectin, fibrinogen, laminin, complement and plasma clotting cascade proteins, a,-antitrypsin, a,-macroglobulin, antichymotrypsin, antithrombin 111, antiplasmin, cystatin C, IgG and IgA, (Grenier, 1996;Pike et al, 1996;Carlsson et al, 1984;Fujimura et al, 1993;Grenier et al, 1989;Lantz et al, 1991;Mayrand & Holt, 1988;Smalley et al, 1989a;Sorsa et a/., 1987;Sundqvist et al, 1985). The major proteolytic activities associated with this organism have been defined by substrate specificity and are ' trypsin-like ', that is cleavage on the carboxyl side of arginyl and lysyl residues (Yoshimura et al, 1984) and collagenolytic (Toda et al, 1984) although other minor activities have been reported (Grenier & Mayrand, 1993).…”

Section: Introductionmentioning

confidence: 99%

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A cell-associated protein complex of Porphyromonas gingivalis W50 composed of Arg- and Lys-specific cysteine proteinases and adhesins

1997

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Porphyromonas gingiwalis has been associated with the development of adult periodontitis and cysteine proteinases with trypsin-like specificity have been implicated as major virulence factors. We have extracted the major cellassociated trypsin-like proteolytic activity of P. gingiwalis W50 using mild sonication. Anion-exchange and gel-f iltration FPLC of the sonicate revealed that Arg-and Lys-specific proteinase activity was associated with a 300 kDa complex which could be dissociated into seven bands (48,45,44,39,27,17 and 15 kDa) by SDS-PAGE with the 4 4 kDa band containing two different proteins as shown by N-terminal sequence analysis. On further chromatography of the 300 kDa complex on ArgSepharose the majority of the complex eluted from the affinity column as an undissociated complex. However, a small amount dissociated such that the Lys-and Arg-specific activities could be separated by eluting first with lysine then arginine, respectively. The 45 kDa protein of the complex was purified by further anion-exchange FPLC in the presence of octylpD-glucopyranoside and was shown to be an Arg-specif ic, thiol-activated, calcium-stabilized cysteine proteinase. The 48 kDa protein was also further purified in a similar fashion and shown to be a Lys-specific cysteine proteinase that was not inhibited by EDTA. The two 44 kDa and the 39,27,17 and 15 kDa proteins of the complex exhibit amino acid sequence homology and are proposed to be haemagglutinindadhesins. The 45 kDa Arg-specif ic proteinase and one of the 44 kDa adhesins as well as the 15,17 and 27 kDa adhesins are processed from the single polyprotein encoded by the gene designated prtR, with all proteins preceded by an Arg or Lys residue within the polyprotein. Similarly, the 48 kDa Lys-specific proteinase, the 39 and 15 kDa adhesins as well as the other 44 kDa adhesin of the 300 kDa complex are encoded by a single gene designated prtK, with all proteins preceded by an Arg or Lys residue within the polyprotein. The 39,15 and 44 kDa adhesins of PrtK all exhibit high homology with the 44,15,17 and 27 kDa adhesins encoded by prtR, particularly the 15 kDa proteins which are identical. The cell-associated proteinase-adhesin complex, designated PrtR-PrtK, is therefore composed of the two gene products, the mature PrtR (160 kDa) and mature PrtK (163 kDa) that are further proteolytically processed (most likely autolytically) to release proteinase and adhesin domains that remain non-covalently associated. The fully processed PrtR-PrtK complex comprises the cysteine proteinases PrtR45 and PrtK48 and seven sequence-related adhesin molecules, PrtR44, PrtRl5, PrtRl7, PrtR27 and PrtK39, PrtK15 and PrtK44. We propose that this proteinase-adhesin complex is a major virulence factor for P. gingiwalis On: Sat, 12 May 2018 21:46:32 P. S. BHOGAL, N. SLAKESKI a n d E. C. REYNOLDS involved in the evasion of host defence and in the assimilation of haem and peptides.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

A cell-associated protein complex of Porphyromonas gingivalis W50 composed of Arg- and Lys-specific cysteine proteinases and adhesins

1997

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“…P. gingivalis has been isolated in great numbers from periodontal pockets of adult patients. P. gingivalis has many potential periodontal pathogens which involve fimbriae, hemagglutinin, LPS, cell-bound and cell-free protease, collagenase, vesicle, and so on (19). It is well known that P. gingivalis releases vesicles into the culture supernatant (20).…”

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confidence: 99%

Effect of Porphyromonas gingivalis ATCC 33277 Vesicle on Adherence of Streptococcus mutans OMZ 70 to the Experimental Pellicle

Kamaguchi

Baba

Hoshi

et al. 1995

Microbiology and Immunology

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The vesicles of Porphyromonas gingivalis ATCC 33277 strongly aggregated Streptococcus cricetus, S. rattus, and S. mutans, but poorly aggregated S. sobrinus. The adherence of S. mutans OMZ 70 to hydroxyapatite (HA) coated with whole saliva was increased in parallel with the quantity of the vesicles. The significant increase of adherence of S. mutans OMZ 70 by the vesicles was also observed on the HA coated with parotid saliva, submandibular saliva, serum, and type I collagen. These findings suggest that the vesicles may act as a bridge between mutans streptococcus and the tooth surface.

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“…Other end-products released by bacteria, such as indole (C 8 H 7 N) and ammonia (NH 3 ), can also be toxic to host cells (77,91).…”

Section: Metabolic End-productsmentioning

confidence: 99%

Bacterial pathogenesis and mediators in apical periodontitis

2007

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Apical periodontitis is a group of inflammatory diseases caused by microorganisms (mainly bacteria) infecting the necrotic root canal system. The pathogenesis of different types of apical periodontitis and even the same type in different individuals is unlikely to follow a stereotyped fashion with regard to the involved bacterial mediators. Disease pathogenesis is rather complex and involves a multitude of bacteria-and host-related factors. This review article discusses the bacterial pathogenesis of acute and chronic apical periodontitis, with the main focus on the bacterial mediators conceivably involved in the different stages of the infectious process, including secreted products (enzymes, exotoxins, N-formyl-methionyl-leucyl-phenylalanine peptides, heat-shock proteins and metabolic end-products) and structural components (lipopolysaccharide, peptidoglycan, lipoteichoic acid, lipoproteins, fimbriae, flagella, outer membrane proteins and vesicles, DNA, and exopolysaccharides). Knowledge of the bacterial factors involved in the pathogenesis of apical periodontitis is important to the understanding of the disease process and to help establishing proper therapeutic measures to inactivate this bacterial "artillery".

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Properties of oral asaccharolytic black-pigmented Bacteroides

Cited by 110 publications

References 8 publications

A cell-associated protein complex of Porphyromonas gingivalis W50 composed of Arg- and Lys-specific cysteine proteinases and adhesins

A cell-associated protein complex of Porphyromonas gingivalis W50 composed of Arg- and Lys-specific cysteine proteinases and adhesins

Effect of Porphyromonas gingivalis ATCC 33277 Vesicle on Adherence of Streptococcus mutans OMZ 70 to the Experimental Pellicle

Bacterial pathogenesis and mediators in apical periodontitis

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