Black‐pigmented Bacteroides from clinically characterized periodontal sites

Spiegel, Carol A.; Hayduk, Susan E.; Minah, Glenn E.; Krywolap, George N.

doi:10.1111/j.1600-0765.1979.tb00234.x

Cited by 157 publications

(76 citation statements)

References 21 publications

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“…Adult periodontitis is strongly associated with infection by Porphyromonas gingivalis (formerly Bacteroides gingivalis) (3)(4)(5)(6)(7), which is further demonstrated by the finding that implantation of this bacterium initiates the progression of periodontitis (8). Proteolytic enzymes, which are produced in large quantity by this bacteria, are considered as important pathogenic agents (9-1 1 ).…”

Section: Introductionmentioning

confidence: 99%

Pathogenesis of periodontitis: a major arginine-specific cysteine proteinase from Porphyromonas gingivalis induces vascular permeability enhancement through activation of the kallikrein/kinin pathway.

Imamura¹,

Pike²,

Potempa³

et al. 1994

J. Clin. Invest.

169

128

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To elucidate the mechanism of production of an inflammatory exudate, gingival crevicular fluid (GCF), from periodontal pockets in periodontitis, we examined the vascular permeability enhancement (VPE) activity induced by an arginine-specific cysteine proteinase, Ar-gingipain-1 (RGP-1), produced by a major periopathogenic bacterium, Porphyromonas gingivalis. Intradermal injections into guinea pigs of RGP-1 (> 10' M), or human plasma incubated with RGP-1 (> 10-9 M), induced VPE in a dose-and activitydependent manner but with different time courses for the two routes of production. VPE activity induced by RGP-1 was augmented by kininase inhibitors, inhibited by a kallikrein inhibitor and unaffected by an antihistamine drug.The VPE activity in human plasma incubated with RGP-1 also correlated closely with generation of bradykinin (BK).RGP-1 induced 30-40% less VPE activity in Hageman factor-deficient plasma and no VPE in plasma deficient in either prekallikrein (PK) or high molecular weight kininogen (HMWK). After incubation with RGP-1, plasma deficient in PK or HMWK, reconstituted with each missing protein, caused VPE, as did a mixture of purified PK and HMVVK, but RGP-1 induced no VPE from HMWK. The VPE of extracts of clinically isolated P. gingivalis were reduced to about 10% by anti-RGP-1-IgG, leupeptin, or tosyl-L-lysine chloromethyl ketone, which paralleled effects observed with RGP-1. These results indicate that RGP-1 is the major VPE factor of P. gingivalis, inducing this activity through PK activation and subsequent BK release, resulting in GCF production at sites of periodontitis caused by infection with this organism. (J. Clin. Invest 1994. 94:361-367.)

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Section: Introductionmentioning

confidence: 99%

Pathogenesis of periodontitis: a major arginine-specific cysteine proteinase from Porphyromonas gingivalis induces vascular permeability enhancement through activation of the kallikrein/kinin pathway.

Imamura¹,

Pike²,

Potempa³

et al. 1994

J. Clin. Invest.

169

128

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“…The numbers and proportion of P. gingivalis generally increase with the development of adult periodontal disease (28,29,32), but the relationship of P. intermedia to periodontal disease is less clear (28,32). P. intermedia may be isolated from healthy and mildly inflamed sites with greater frequency than P. gingivalis (28,32), suggesting an ecological distinction between the two organisms.…”

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confidence: 99%

Detection and comparison of specific hemin binding by Porphyromonas gingivalis and Prevotella intermedia

1997

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A radioligand assay was designed to detect and compare specific hemin binding by the periodontal anaerobic black-pigmenting bacteria (BPB) Porphyromonas gingivalis and Prevotella intermedia. The assay included physiological concentrations of the hemin-binding protein rabbit serum albumin (RSA) to prevent self-aggregation and nonspecific interaction of hemin with cellular components. Under these conditions, heme-starved P. intermedia cells (two strains) expressed a single binding site species (4,100 to 4,600 sites/cell) with a dissociation constant (K d ) of 1.0 ؋ 10 ؊9 M. Heme-starved P. gingivalis cells (two strains) expressed two binding site species; the higher-affinity site (1,000 to 1,500 sites/cell) displayed a K d of between 3.6 ؋ 10 ؊11 and 9.6 ؋ 10 ؊11 M, whereas the estimated K d of the lower-affinity site (1.9 ؋ 10 5 to 6.3 ؋ 10 5 sites/cell) ranged between 2.6 ؋ 10 ؊7 and 6.5 ؋ 10 ؊8 M. Specific binding was greatly diminished in heme-replete cells of either BPB species and was not displayed by iron-replete Escherichia coli cells, which bound as much hemin in the absence of RSA as did P. intermedia. Hemin binding by BPB was reduced following treatment with protein-modifying agents (heat, pronase, and N-bromosuccinimide) and was blocked by protoporphyrin IX and hemoglobin but not by Congo red. Hemopexin also inhibited bacterial hemin binding. These findings indicate that both P. gingivalis and P. intermedia express heme-repressible proteinaceous hemin-binding sites with affinities intermediate between those of serum albumin and hemopexin. P. gingivalis exhibited a 10-fold-greater specific binding affinity and greater heme storage capacity than did P. intermedia, suggesting that the former would be ecologically advantaged with respect to heme acquisition.

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“…Representatives of Bacteroides melaninogenicus have been isolated from disease processes in the mouth (Spiegel et al, 1979) and from other sites (Smith, 1975;Finegold, 1977). B. gingivalis, which is composed of mainly oral strains that were formerly assigned to B. asaccharolyticus (Coykendall, Kaczmarek and Slots, 1980;van Steenbergen, Vlaanderen and de Graaff, 1981), seems to be very important in adult periodontitis (Slots, 1979;Spiegel et a!., 1979;Tanner et al, 1979). The strains still classed as B. asaccharolyticus can be isolated from infections away from the mouth (Smith, 1975;Finegold, 1977).…”

Section: Introductionmentioning

confidence: 99%

Cytotoxic Activity of Bacteroides Gingivalis and Bacteroides Asaccharolyticus

Steenbergen¹,

Ouden²,

Touw³

et al. 1982

Journal of Medical Microbiology

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SUMMARY. Culture filtrates of all eight strains of Bacteroides gingivalis and all five strains of B. asaccharolyticus were toxic for Vero cells. Cytotoxicity was in general greater with material from cultures of B. gingivalis than from B. asaccharolyticus but none of the culture filtrates from eight strains of B. melaninogenicus showed activity in this test. The toxic material was released during prolonged incubation and more detailed study of preparations from one strain indicated that it had a molecular weight of less than 3500 and was heat stable.

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Black‐pigmented Bacteroides from clinically characterized periodontal sites

Cited by 157 publications

References 21 publications

Pathogenesis of periodontitis: a major arginine-specific cysteine proteinase from Porphyromonas gingivalis induces vascular permeability enhancement through activation of the kallikrein/kinin pathway.

Pathogenesis of periodontitis: a major arginine-specific cysteine proteinase from Porphyromonas gingivalis induces vascular permeability enhancement through activation of the kallikrein/kinin pathway.

Detection and comparison of specific hemin binding by Porphyromonas gingivalis and Prevotella intermedia

Cytotoxic Activity of Bacteroides Gingivalis and Bacteroides Asaccharolyticus

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