Molecular analysis of periodontal pathogens

Lawson, David A.; Haas, R; Meyle, Joerg; Meyer, Thomas F.

doi:10.1016/0003-9969(90)90138-z

Cited by 3 publications

(2 citation statements)

References 12 publications

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“…Studies 4,5 have addressed the mechanisms of periodontal destruction, especially those of gingiva and alveolar bone by these periodontopathic bacteria. Periodontal bacteria form a biofilm in the periodontal pocket, and the biofilm directly or indirectly damages the periodontium by producing or inducing the production of various kinds of enzymes and/or exotoxins 6 . The biofilm is complex, with bacterial extracellular polymeric substances; 7–9 and its construction is so dense that antimicrobial agents can barely penetrate its full depth.…”

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confidence: 99%

One‐Stage Full‐Mouth Versus Partial‐Mouth Scaling and Root Planing During the Effective Half‐Life of Systemically Administered Azithromycin

Yashima

Gomi

Maeda

et al. 2009

Journal of Periodontology

105

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confidence: 99%

One‐Stage Full‐Mouth Versus Partial‐Mouth Scaling and Root Planing During the Effective Half‐Life of Systemically Administered Azithromycin

Yashima

Gomi

Maeda

et al. 2009

Journal of Periodontology

105

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“…Proteases capable of degrading collagen, fibrinogen, fibronectin and other host proteins have a central role in the bacterial infection and tissue destruction of periodontai diseases. Since purification of these bacterial enzymes has been difficult and incomplete, molecular biology offers alternative methods for their study (27), In this study we have cloned, expressed and characterized P. gitigivalis proteolytic activity with broad substrate specificity. However, it is clear that when high levels of this proteolytic activity are expressed in E. coli, it is a lethal event, resulting in instability of the clone.…”

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confidence: 99%

Expression of Porphyromonas gingivalis proteolytic activity in Escherichia coli

Madden

Thompson

Clark

1992

Oral Microbiology and Immunology

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Porphyromonas gingivalis (formerly Bacteroides gingivalis) degrades numerous protein substrates including collagen, fibrinogen, fibronectin, gelatin, casein, immunoglobulins and complement components. In order to clone one or more of these protease genes, a genomic library was constructed with Sau3A1 restriction fragments of chromosomal DNA from P. gingivalis ATCC 33277 ligated into the temperature-regulated vector pCQV2, and expressed in Escherichia coli DH5 alpha mcr. The electro-transformants (3 x 10(4)) were screened for general protease activity on Luria broth agar containing ampicillin (50 mg/l) and sodium caseinate (2%). One casein-hydrolyzing clone was detected and subcultured, and the activity of the cell extracts was characterized. We were able to show that the protease-positive clone, (pTEM1), had broad substrate specificity. Colorimetric assays indicated the hydrolysis of azocoll, azocasein, collagen, elastin-congo red and artificial substrates. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis was used to confirm that collagen, casein, fibrinogen and fibronectin were degraded by the clone.

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Identification of Actinobacillus actinomycetemcomitans by leukotoxin gene-specific hybridization and polymerase chain reaction assays

Tønjum

Haas

1993

J Clin Microbiol

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Eleven strains of Actinobacilus actinomycetemcomitans isolated from cases of systemic infections, local abscesses, and periodontitis were identified by genetic assays using the leukotoxin gene as the target. We have developed a polymerase chain reaction (PCR) assay, based on the leukotoxin structural gene of this pathogen, which clearly identified all tested strains of A. actinomycetemcomitans and separated them from the closely related Haemophilus aphrophilus as well as other bacterial species. Furthermore, DNA-DNA hybridization was performed with the cloned partial leukotoxin structural gene (lktA) as a probe, which again clearly distinguished A. actinomycetemcomitans from H. aphrophilus, parts of the normal oral flora, and species harboring RTX (repeats in toxin) family-related cytotoxins. The PCR fragment amplified from the leukotoxin structural gene gave results similar to those given by the cloned leukotoxin gene when used as a probe in hybridization experiments. The hybridization and PCR assays described here are fundamental improvements for the identification of A. actinomycetemcomitans.

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Molecular analysis of periodontal pathogens

Cited by 3 publications

References 12 publications

One‐Stage Full‐Mouth Versus Partial‐Mouth Scaling and Root Planing During the Effective Half‐Life of Systemically Administered Azithromycin

One‐Stage Full‐Mouth Versus Partial‐Mouth Scaling and Root Planing During the Effective Half‐Life of Systemically Administered Azithromycin

Expression of Porphyromonas gingivalis proteolytic activity in Escherichia coli

Identification of Actinobacillus actinomycetemcomitans by leukotoxin gene-specific hybridization and polymerase chain reaction assays

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