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PubMed2002

Proteolysis of interleukin-6 receptor (IL-6R) by Porphyromonas gingivalis cysteine proteinases (gingipains) inhibits interleukin-6-mediated cell activation.

Current consensus is that periodontitis is an infectious disease in which a deregulated chronic inflammatory reaction not only may lead to periodontal tissue damage but also eventually may cause tooth loss. In controlling the inflammatory state the interplay between a network of cytokines and their receptors plays an important role. Here we show that the interleukin-6 receptor (IL-6R) is rapidly and efficiently inactivated by gingipains, the arginine- (HRgpA and RgpB) and lysine- (Kgp) specific cysteine proteinases from Porphyromonas gingivalis. Preincubation of HepG2 cells with active gingipains results in the loss of gp80 (CD126) from the cell surface. This also correlates with a decreased responsiveness to stimulation by interleukin-6 (IL-6), as determined by measurement of the status of IL-6R-mediated STAT 3 (Signal Transducer and Activator of Transcription 3) activation by this cytokine. Significantly, incubation of cells with gingipains was not accompanied by release of the soluble receptor, indicating its degradation, and this was confirmed by susceptibility of the recombinant, soluble receptor to proteolytic digestion by these enzymes. With the exception of the degradation of soluble IL-6R (sIL-6R) by Kgp, all of these reactions were also observed in the presence of serum suggesting that receptor inactivation may occur in vivo. Interestingly, Kgp, although less effective in cleaving sIL-6R, was able to decrease cell responsiveness to IL-6, possibly through degradation/inactivation of the signal transducing component (gp130) associated with IL-6R. These data, together with previous observation that IL-6 itself is inactivated by gingipains, suggest that at periodontitis sites infected by P. gingivalis the inflammatory reactions dependent on IL-6 could be severely hindered contributing to both tissue damage and periodontopathogen survival.

Adhesins, Bacterial↗
PubMed2000

The role of bacterial and host proteinases in periodontal disease.

It is abundantly obvious that the uncontrolled degradation and/or activation of host defense pathways is the major pathway by which the periodontal pathogen P. gingivalis promotes its growth and proliferation. By being able to shed host receptors, degrade cytokines, and activate coagulation, complement, and kallikrein/kinin pathways it is clear that this organism has found a mechanism(s) to evade host defense and at the same time develop a system for cannibalizing host proteins for its own nutritional usage (Fig 2). Thus, it seems only logical that the development of inhibitors against these bacterial proteinases would be a useful method for negating their activities and making such pathogens more susceptible to attack by host phagocyte cells. In this respect, the structure of the truncated form of RGP has just been elucidated. Thus, it should only be a question of time before inhibitors to this enzyme will be developed and, hopefully, be used to reduce the pathologies associated with the development of periodontitis and/or eliminate the disease altogether.

Adhesins, Bacterial↗
PubMed1989

Cloning and sequencing of an endoglucanase (end1) gene from Butyrivibrio fibrisolvens H17c.

The nucleotide sequence of a 2.8 kb DNA segment containing an endoglucanase gene (end1) from Butyrivibrio fibrisolvens H17c was determined. The B. fibrisolvens H17c gene was expressed from its own regulatory region in Escherichia coli and three putative consensus promoter sequences were identified upstream of a ribosome binding site and an ATG start codon. The complete amino acid sequence (547 residues) was deduced and homology with the Clostridium thermocellum celE gene product (EGE) was demonstrated. The endoglucanase contained a typical amino-terminal signal sequence and five repeated sequences (PDPTPVD) between amino acids 412-447. The endoglucanase showed relatively high endoglucanase activity against endoglucanase-specific substrates with beta 1-4 linkages but low activity against xylan and an exoglucanase-specific substrate, p-nitrophenyl-beta-D-cellobioside.

Amino Acid Sequence↗
PubMed1990

Sequencing and expression of a cellodextrinase (ced1) gene from Butyrivibrio fibrisolvens H17c cloned in Escherichia coli.

The nucleotide sequence of a 2.314 kb DNA segment containing a gene (ced1) expressing cellodextrinase activity from Butyrivibrio fibrisolvens H17c was determined. The B. fibrisolvens H17c gene was expressed from a weak internal promoter in Escherichia coli and a putative consensus promoter sequence was identified upstream of a ribosome binding site and a GTG start codon. The complete amino acid sequence (547 residues) was deduced and homology was demonstrated with the Clostridium thermocellum endoglucanase D (EGD), Pseudomonas fluorescens var. cellulosa endoglucanase (EG), and a cellulase from the avocado fruit (Persea americana). The ced1 gene product Ced1 showed cellodextrinase activity and rapidly hydrolysed short-chain cellodextrins to yield either cellobiose or cellobiose and glucose as end products. The Ced1 enzyme released cellobiose from p-nitrophenyl-beta-D-cellobioside and the enzyme was not inhibited by methylcellulose, an inhibitor of endoglucanase activity. Although the major activity of the Ced1 enzyme was that of a cellodextrinase it also showed limited activity against endoglucanase specific substrates [carboxymethylcellulose (CMC), lichenan, laminarin and xylan]. Analysis by SDS-polyacrylamide gel electrophoresis with incorporated CMC showed a major activity band with an apparent Mr of approximately 61,000. The calculated Mr of the ced1 gene product was 61,023.

Amino Acid Sequence↗
PubMed1990

The fumarate reductase operon of Wolinella succinogenes. Sequence and expression of the frdA and frdB genes.

The genes of the fumarate reductase of Wolinella succinogenes are organized in an operon. The three structural genes in the order frdC, frdA, frdB, are preceded by a common promoter (Körtner et al. 1990) and followed by a terminator of transcription. The proteins encoded by the genes are identical with the subunits present in the isolated enzyme. FrdA and FrdB are hydrophilic proteins consisting of 656 and 238 amino acids, respectively. The 12 cysteine residues present in FrdB form 3 ferredoxin-like clusters, whereas the 12 cysteines of FrdA are not clustered. Expression of FrdA and FrdB in Escherichia coli from a plasmid containing a DNA fragment with both genes in full length, gave rise to the EPR signals of the bi- and trinuclear iron-sulfur centers of the enzyme. Only the binuclear center was seen on the expression of FrdB together with a C-terminal fragment of FrdA (130 amino acid residues). Neither of the two centers was detected on the expression of FrdA together with a N-terminal fragment of FrdB including cysteine cluster I. Sequence comparison of FrdA and FrdB with the corresponding subunits of the fumarate reductases of E. coli or Proteus vulgaris or to those of the succinate dehydrogenases of E. coli or Bacillus subtilis revealed strong homologies (28-36% identical amino acid residues). Part of the homologous peptide stretches could be assigned to domains that are involved in the binding of the substrate of the FAD prosthetic group of the enzyme.

Amino Acid Sequence↗
PubMed1991

Cloning, sequencing and expression of a gene encoding a 73 kDa xylanase enzyme from the rumen anaerobe Butyrivibrio fibrisolvens H17c.

The cloning, expression and nucleotide sequence of a 3 kb DNA segment on pLS206 containing a xylanase gene (xynB) from Butyrivibrio fibrisolvens H17c was investigated. The open reading frame (ORF) of 1905 bp encoded a xylanase of 635 amino acid residues (Mr 73156). At least 850 bp at the 3' end of the gene could be deleted without loss of xylanase activity. The deduced amino acid sequence was confirmed by purifying the enzyme and subjecting it to N-terminal amino acid sequence analysis. In Escherichia coli C600 (pLS206) cells the xylanase was localized in the cytoplasm. Its optimum pH for activity was between pH 5.4 and 6, and optimum temperature 55 degrees C. The primary structure of the xylanase showed a significant level of identity with a cellobiohydrolase/endoglucanase of Caldocellum saccharolyticum, as well as with the xylanases of the alkaliphilic Bacillus sp. strain C-125, B. fibrisolvens strain 49, and Pseudomonas fluorescens subsp. cellulosa.

Amino Acid Sequence↗
PubMed1994

Expression of the Butyrivibrio fibrisolvens endo-beta-1,4-glucanase gene together with the Erwinia pectate lyase and polygalacturonase genes in Saccharomyces cerevisiae.

Recombinant Saccharomyces cerevisiae strains capable of simultaneous secretion of bacterial glucanase and pectinase enzymes have been developed. The Butyrivibrio fibrrisolvens endo-beta-1,4-glucanase gene (end1), the Erwinia chrysanthemi pectate lyase gene (pelE) and E. carotovora polygalacturonase gene (peh1) were each inserted between a yeast expression-secretion cassette and yeast gene terminator, and cloned into yeast-centromeric shuttle vectors. Transcription initiation signals present in the expression-secretion cassette were derived from the yeast alcohol dehydrogenase gene promoter (ADC1P), whereas the transcription termination signals were derived from the yeast tryptophan synthase gene terminator (TRP5T). Secretion of glucanase and pectinases was directed by the signal sequence of the yeast mating pheromone alpha-factor (MF alpha 1S). These YCplac111-based constructs, designated END1, PEL5, AND PEH1, respectively, were transformed into S. cerevisiae. The END1, PEL5 and PEH1 constructs were co-expressed in laboratory strains of S. cerevisiae as well as in wine and distillers' yeasts. DNA-RNA hybridization analysis showed the presence of END1, PEL5 and PEH1 transcripts. Carboxymethylcellulose and polypectate agarose assays revealed the production of biologically active endo-beta-1,4-glucanase, pectate lyase and polygalacturonase by the S. cerevisiae transformants. Interestingly, although the same expression-secretion cassette was used in all three constructs, time-course assays indicated that the pectinases were secreted before the glucanase. It is tempting to speculate that the bulkiness of the END1-encoded protein and the five alternating repeats of Pro-Asp-Pro-Thr(Gln)-Pro-Val-Asp within the glucanase moiety could be involved in the delayed secretion of the glucanase.

Amino Acid Sequence↗
PubMed1990

The problem of the taxonomy of the fusiform bacillus of acute necrotizing ulcerative gingivitis (Vincent's gingivitis).

The characteristic microscopic appearance of the fusospirochaetal complex in smears from patients with acute necrotizing ulcerative gingivitis has long been regarded as virtually pathognomonic of the disease. Unfortunately there is considerable confusion surrounding the taxonomy of the fusiform organism in the fusospirochaetal complex. The conflicting views appear to be irreconcilable and a re-evaluation of the taxonomy of oral fusiforms is urgently required.

Bacteroidaceae↗
PubMed1985

Oxalobacter formigenes gen. nov., sp. nov.: oxalate-degrading anaerobes that inhabit the gastrointestinal tract.

This report describes a new group of anaerobic bacteria that degrade oxalic acid. The new genus and species, Oxalobacter formigenes, are inhabitants of the rumen and also of the large bowel of man and other animals where their actions in destruction of oxalic acid may be of considerable importance to the host. Isolates from the rumen of a sheep, the cecum of a pig, and from human feces were all similar Gram-negative, obligately anaerobic rods, but differences between isolates in cellular fatty acid composition and in serologic reaction were noted. Measurements made with type strain OxB indicated that 1 mol of protons was consumed per mol of oxalate degraded to produce approximately 1 mol of CO2 and 0.9 mol of formate. Substances that replaced oxalate as a growth substrate were not found.

Animals↗
PubMed1980

Factors contributing to loss of anaerobic bacteria in transit from the patient to the laboratory.

Care and attention to detail in the sampling, transit and submission of a specimen for anaerobic bacteriological investigation are of paramount importance. The swab is a relatively inefficient sampling device and is often abused. A transport system may help, but a full evaluation of our sampling and transport methodology is needed and this will be influenced by local circumstances.

Anaerobiosis↗
PubMed1980

Diagnosis and therapy of anaerobic infections in childhood.

There are two main periods of manifestation of anaerobic infections in childhood. In the neonatal period anaerobic septicaemia is usually mild with a lower mortality rate, but has essentially the same causes as aerobic septicaemia (premature rupture of the membranes, amniotic infection syndrome after ascending infection). The latter cases comprise about 10% of aerobic septicaemias. Later in childhood, the pathogenesis of anaerobic infections is similar to that in adulthood. Anaerobic infections occur after surgery, particularly of the abdominal region, in malignancies, immunodeficiency and aspiration. With the exception of Bacteroides fragilis, most anaerobes are sensitive to penicillin. A high percentage of clinically important anaerobes are sensitive to clindamycin, chloramphenicol and metronidazole.

Anaerobiosis↗
PubMedDate not supplied

Newly delineated periodontal pathogens with special reference to selenomonas species.

Many new species have been isolated from subgingival periodontal pockets, for example Wolinella recta and Bacteroides forsythus, reflecting better basic microbiological techniques. Other species were created from existing species as a result of better characterization methods, i.e. Bacteroides buccae and Bacteroides oris. We can recognize different types of periodontal disease and can find differences relating to the progressive compared to inactive lesions. Data illustrated in this presentation suggest that potential pathogens within new species include B. forsythus, W. recta and quite probably Selenomonas noxia. Methods that are rapid and sensitive for these new species include the use of protein profiles determined using SDS-PAGE, and DNA probes.

Bacterial Infections↗
PubMedDate not supplied

Etiological agents and predisposing factors of intracranial abscesses in a Greek university hospital.

The bacteriology for 21 patients with brain abscesses is presented and correlated with their predisposing conditions. Chronic otomastoiditis was the most common predisposing factor, and the overall most frequent infected sites were the frontal and temporal regions. Gram-negative non-sporeforming anaerobes of the genus Bacteroides and Fusobacterlum followed by aerobic streptococci were the predominant pathogens. Enterobacteria were only identified in postcraniotomy abscesses, while a substantial number of fastidious species was detected in suppurations related to congenital heart disease. Altogether, anaerobes alone were recovered in seven patients, aerobes alone in six, and mixed aerobes and anaerobes in four patients. These findings confirm the predominant role of anaerobes in the etiology of intracranial suppurations.

Adolescent↗
PubMed1992

beta-Lactamase production and susceptibility of US and European anaerobic gram-negative bacilli to beta-lactams and other agents.

The susceptibility of 1,476 US and European strains of anaerobic gram-negative bacilli to amoxicillin, amoxicillin/clavulanate, ticarcillin, ticarcillin/clavulanate, cefoxitin, imipenem and metronidazole was determined. All of the Bacteroides fragilis group and 51% of the non-Bacteroides fragilis group were beta-lactamase positive. Amongst the non-Bacteroides fragilis group, beta-lactamase positivity rates were higher for US strains (58%) than for European strains (39%). All strains were susceptible to imipenem and metronidazole. MIC90s of amoxicillin and ticarcillin for all beta-lactamase negative strains were 0.5 and 2 micrograms/ml, respectively. The addition of clavulanate reduced the MIC90s of amoxicillin (> or = 256 micrograms/ml) and ticarcillin (> or = 64 micrograms/ml) to 16 and 8 micrograms/ml, respectively, for the Bacteroides fragilis group, and to 4 micrograms/ml for both agents for the non-Bacteroides fragilis beta-lactamase producing group. Twenty-nine cefoxitin-resistant strains were found, mainly in the Bacteroides fragilis group, while 95 beta-lactamase producing strains (predominantly Bacteroides fragilis group and fusobacteria) did not show synergy between beta-lactams and clavulanate. Of the newe agents tested, meropenem and piperacillin-tazobactam were the most active (100% of strains susceptible), followed by amoxicillin-BRL 42715 (99% of strains susceptible); 94 to 98% of the strains were susceptible to cefoperazone-sulbactam, tosufloxacin, temafloxacin and clindamycin. Only 73% of the strains were susceptible to cefotetan, compared to 91% to cefoxitin; 88% of the strains were susceptible to trospectomycin. Overall, all of the beta-lactam/beta-lactamase inhibitor combinations, imipenem, meropenem, cefoxitin, tosufloxacin, temafloxacin and clindamycin had good activity against beta-lactamase producing strains, while all agents tested had good activity against beta-lactamase negative strains.

Anti-Bacterial Agents↗
PubMed1984

Pyogenic liver abscess: diagnosis, bacteriology and treatment.

Pyogenic liver abscess is an uncommon but potentially fatal disease. The accuracy of diagnosis made on clinical grounds can now be greatly improved with the use of modern organ-imaging techniques. The condition is often polymicrobial: Escherichia coli and other enteric gram-negative rods are major pathogens, with anaerobic gram-negative rods and Streptococcus milleri being increasingly recognised. Staphylococcal liver abscesses are less common, often arising in association with neutrophil disorders. Open surgical drainage along with antimicrobial chemotherapy has long been regarded as standard treatment, however, in many centres it is being displaced by percutaneous drainage under the guidance of computed tomography or ultrasound. Some patients have been successfully treated with antimicrobial chemotherapy alone. Once specimens have been taken for culture, empiric antimicrobial therapy should include a combination of an anti-anaerobe agent, an aminoglycoside and a beta-lactam drug such as ampicillin. Early diagnosis and treatment of this condition is essential for patient survival.

Anti-Bacterial Agents↗
PubMed1999

Alternative schemes of butyrate production in Butyrivibrio fibrisolvens and their relationship to acetate utilization, lactate production, and phylogeny.

Butyrivibrio fibrisolvens strains D1 and A38 produced little lactate, but strain 49 converted as much as 75% of its glucose to lactate. Strain 49 had tenfold more lactate dehydrogenase activity than strains D1 or A38, this activity was stimulated by fructose 1,6-bisphosphate, and had a pH optimum of 6.25. A role for fructose 1,6-bisphosphate or pH regulation of lactate production in strain 49 was, however, contradicted by the observations that very low concentrations (< 0.2 mM) of fructose 1,6-bisphosphate gave maximal activity, and continuous cultures did not produce additional lactate when the pH was decreased. The lactate production of strain 49 was clearly inhibited by the presence of acetate in the growth medium. When strain 49 was supplemented with as little as 5 mM acetate, lactate production decreased dramatically, and most of the glucose was converted to butyrate. Strain 49 did not possess butyrate kinase activity, but it had a butyryl-CoA/acetate CoA transferase that converted butyryl-CoA directly to butyrate, using acetate as an acceptor. The transferase had a low affinity for acetate (K(m) of 5 mM), and this characteristic explained the acetate stimulation of growth and butyrate formation. Strains D1 and A38 had butyrate kinase but not butyryl-CoA/acetate CoA transferase, and it appeared that this difference could explain the lack of acetate stimulation and lactate production. Based on these results, it is unlikely that B. fibrisolvens would ever contribute significantly to the pool of ruminal lactate. Since relatives of strain 49 (strains Nor37, PI-7, VV1, and OB156, based on 16S rRNA sequence analysis) all had the same method of butyrate production, it appeared that butyryl-CoA/acetate CoA transferase might be a phylogenetic characteristic. We obtained a culture of strain B835 (NCDO 2398) that produced large amounts of lactate and had butyryl-CoA/acetate CoA transferase activity, but this strain had previously been grouped with strains A38 and D1 based on 16S rRNA sequence analysis. Our strain B835 had a 16S rRNA sequence unique from the one currently deposited in GenBank, and had high sequence similarity with strains 49 and Nor37 rather than with strains A38 or D1.

Acetates↗