PubMed Health⌕ Search

SEARCH · PubMed Health

Results for “Enterococcus faecalis”

Explore indexed PubMed citations for clinical trials, systematic reviews and public health research. Read source abstracts and follow each citation to its original PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 829 records · Page 46Linked to original sources

Spontaneous vegetative endocarditis due to Enterococcus faecalis in a rottweiler puppy.

A 5-month-old female Rottweiler was referred because of a 5-week diarrhea and a sudden onset of a cardiac murmur auscultated by its veterinarian. Definitive diagnosis of bacterial endocarditis was based on ultrasonographic visualization of vegetative cardiac lesions and positive cultures of Enterococcus faecalis in blood and urine. Complicating findings were suppurative nephritis and renal infarction. Despite intensive supportive care, the endocarditis and clinical condition deteriorated and the dog had to be euthanized.

Animals↗

[Reduction of acute recurrence in patients with chronic recurrent hypertrophic sinusitis by treatment with a bacterial immunostimulant (Enterococcus faecalis Bacteriae of human origin].

A double-blind, placebo-controlled multicenter study in 157 patients with chronic recurrent sinusitis investigated the occurrence of acute relapses during treatment of patients with a bacterial immunostimulant (3 x 30 drops/day), comprised of cells and autolysate of human Enterococcus faecalis bacteria (Symbioflor 1, n = 78) in comparison to placebo (n = 79). The study included a treatment period of 6 months and a follow-up period of 8 months. Under verum the occurrence of relapses (50 incidents) was about half (56%) the number observed under placebo (90 incidents). In the Kaplan-Meier test the verum preparation emerged as significantly superior (p = 0.045, log rank test) compared to placebo. This superiority of verum was found during the treatment period with 17 vs. 33 relapses (p = 0.019) as well as during the follow-up observation with 33 vs. 57 relapses (p = 0.013). The time interval to the first relapse was clearly longer under verum (513 days) than under placebo (311 days). The relative risk for a relapse under the test preparation compared to placebo was 49.0% during the treatment and 55.8% during the follow-up period. Severity of the acute relapses was comparable in both groups. However, antibiotic therapy was only required in 2 patients treated with verum compared to 6 patients in the placebo group. Both preparations were well tolerated and serious side effects did not occur in either group. No changes in laboratory tests--hematology and clinical chemistry--were observed. Potential immunomodifying effects of the test preparation in view of the significant reduction in relapses were discussed.

Adjuvants, Immunologic↗

The hprK gene of Enterococcus faecalis encodes a novel bifunctional enzyme: the HPr kinase/phosphatase.

The HPr kinase of Gram-positive bacteria is an ATP-dependent serine protein kinase, which phosphorylates the HPr protein of the bacterial phosphotransferase system (PTS) and is involved in the regulation of carbohydrate metabolism. The hprK gene from Enterococcus faecalis was cloned via polymerase chain reaction (PCR) and sequenced. The deduced amino acid sequence was confirmed by microscale Edman degradation and mass spectrometry combined with collision-induced dissociation of tryptic peptides derived from the HPr kinase of E. faecalis. The gene was overexpressed in Escherichia coli, which does not contain any ATP-dependent HPr kinase or phosphatase activity. The homogeneous recombinant protein exhibits the expected HPr kinase activity as well as a P-Ser-HPr phosphatase activity, which was assumed to be a separate enzyme activity. The bifunctional HPr kinase/phosphatase acts preferentially as a kinase at high ATP levels of 2 mM occurring in glucose-metabolizing Streptococci. At low ATP levels, the enzyme hydrolyses P-Ser-HPr. In addition, high concentrations of phosphate present under starvation conditions inhibit the HPr kinase activity. Thus, a putative function of the enzyme may be to adjust the ratio of HPr and P-Ser-HPr according to the metabolic state of the cell; P-Ser-HPr is involved in carbon catabolite repression and regulates sugar uptake via the phosphotransferase system (PTS). Reinvestigation of the previously described Bacillus subtilis HPr kinase revealed that it also possesses P-Ser-HPr phosphatase activity. However, contrary to the E. faecalis enzyme, ATP alone was not sufficient to switch the phosphatase activity of the B. subtilis enzyme to the kinase activity. A change in activity of the B. subtilis HPr kinase was only observed when fructose-1,6-bisphosphate was also present.

Bacillus subtilis↗

Enterococcus faecalis causing empyema in a patient with liver disease.

A 57-year-old man with a history of liver disease had shortness of breath, fever, and pleuritic chest pain. Ascites was not present. Computed tomography (CT) of the chest revealed a large unilateral pleural effusion, compressive atelectasis, and no evidence of consolidation. Culture of the pleural fluid grew Enterococcus faecalis. Treatment with ampicillin in conjunction with tube thoracostomy resulted in clinical improvement. This case illustrates the development of spontaneous monomicrobial empyema due to E. faecalis in a patient with liver disease, in the absence of pneumonia and peritonitis.

Empyema, Pleural↗

Enterococcus faecalis mevalonate kinase.

Gram-positive pathogens synthesize isopentenyl diphosphate, the five-carbon precursor of isoprenoids, via the mevalonate pathway. The enzymes of this pathway are essential for the survival of these organisms, and thus may represent possible targets for drug design. To extend our investigation of the mevalonate pathway in Enterococcus faecalis, we PCR-amplified and cloned into pET-28b the mvaK1 gene thought to encode mevalonate kinase, the fourth enzyme of the pathway. Following transformation of the construct EFK1-pET28b into Escherichia coli BL21(DE3) cells, the expressed C-terminally hexahistidine-tagged protein was purified on a nickel affinity support to apparent homogeneity. The purified protein catalyzed the divalent ion-dependent phosphorylation of mevalonate to mevalonate 5-phosphate. The specific activity of the purified kinase was 24 micromole/min/mg protein. Based on sedimentation velocity data, E. faecalis mevalonate kinase exists in solution primarily as a monomer with a mass of 32.2 kD. Optimal activity occurred at pH 10 and at 37 degrees C. Delta H(a) was 22 kcal/mole. Kinetic analysis suggested that the reaction proceeds via a sequential mechanism. K(m) values were 0.33 mM (mevalonate), 1.1 mM (ATP), and 3.3 mM (Mg(2+)). Unlike mammalian mevalonate kinases, E. faecalis mevalonate kinase utilized all tested nucleoside triphosphates as phosphoryl donors. ADP, but not AMP, inhibited the reaction with a K(i) of 2.7 mM.

Adenosine Diphosphate↗

Conjugative plasmid transfer from Enterococcus faecalis to Escherichia coli.

The possibility of transfer of genetic information by conjugation from gram-positive to gram-negative bacteria was investigated with a pBR322-pAM beta 1 chimeric plasmid, designated pAT191. This shuttle vector, which possesses the tra functions of the streptococcal plasmid pAM beta 1, was conjugatively transferred from Enterococcus faecalis to Escherichia coli with an average frequency of 5 x 10(-9) per donor colony formed after mating.

Conjugation, Genetic↗

In vivo transfer of pAM beta 1 from Lactobacillus reuteri to Enterococcus faecalis.

Trials were conducted to determine the in vivo transferability of plasmid-mediated antibiotic resistance between two strains of enteric Gram-positive bacteria. Germ-free mice were associated with the donor Lactobacillus reuteri DSM 20016 strain, carrying the broad host range pAM beta 1 plasmid, and with the Enterococcus faecalis JH2SS recipient strain. Analysis of faecal content of associated mice demonstrated that the in vivo transfer of this plasmid did occur and that frequencies of conjugation were affected by the presence of subtherapeutic levels of antibiotic in the diet.

Animals↗

Dentin enhances the effectiveness of bioactive glass S53P4 against a strain of Enterococcus faecalis.

OBJECTIVE: The aim of the current study was to test the impact of dentin powder on the antimicrobial efficacy of bioactive glass S53P4 (BAG). STUDY DESIGN: BAG was suspended (preincubated) in saline at 37 degrees C for different time periods with or without human dentin powder, hydroxylapatite, or decalcified dentin. Subsequently, Enterococcus faecalis ATCC 29212 cells were added to these suspensions and bacterial recovery measured with and without the use of gentle sonication. Furthermore, survival of bacteria in test and control suspensions was assessed over time. Supernatants of suspensions were analyzed for their element contents using atomic absorption spectrophotometry. The effects of pH, silica, and osmolarity on E faecalis viability were assessed using specifically prepared solutions. RESULTS: BAG preincubated with dentin powder caused a significant (P < .05) decrease in viability compared to pure BAG suspensions. This was not based on adherence of bacteria to solid particles or agglutination of the cells, because sonication did not increase bacterial yields. Hydroxylapatite and decalcified dentin did not increase BAG killing efficacy. The additive effect of BAG + dentin powder was dose dependent, occurred only with solids in suspension, and increased with suspension time. An augmented dissolution of glass components, especially silicon, was measured in BAG + dentin powder compared to pure BAG suspensions or counterparts containing hydroxylapatite or decalcified dentin. High osmolarity per se did not affect E faecalis viability, whereas high pH and silica levels did. CONCLUSION: The observed phenomenon was related to an increased BAG dissolution triggered by dentin powder, causing elevated local pH and silica levels.

Anti-Infective Agents, Local↗

Enterococcus faecalis phosphomevalonate kinase.

The six enzymes of the mevalonate pathway of isopentenyl diphosphate biosynthesis represent potential for addressing a pressing human health concern, the development of antibiotics against resistant strains of the Gram-positive streptococci. We previously characterized the first four of the mevalonate pathway enzymes of Enterococcus faecalis, and here characterize the fifth, phosphomevalonate kinase (E.C. 2.7.4.2). E. faecalis genomic DNA and the polymerase chain reaction were used to clone DNA thought to encode phosphomevalonate kinase into pET28b(+). Double-stranded DNA sequencing verified the sequence of the recombinant gene. The encoded N-terminal hexahistidine-tagged protein was expressed in Escherichia coli with induction by isopropylthiogalactoside and purified by Ni(++) affinity chromatography, yield 20 mg protein per liter. Analysis of the purified protein by MALDI-TOF mass spectrometry established it as E. faecalis phosphomevalonate kinase. Analytical ultracentrifugation revealed that the kinase exists in solution primarily as a dimer. Assay for phosphomevalonate kinase activity used pyruvate kinase and lactate dehydrogenase to couple the formation of ADP to the oxidation of NADH. Optimal activity occurred at pH 8.0 and at 37 degrees C. The activation energy was approximately 5.6 kcal/mol. Activity with Mn(++), the preferred cation, was optimal at about 4 mM. Relative rates using different phosphoryl donors were 100 (ATP), 3.6 (GTP), 1.6 (TTP), and 0.4 (CTP). K(m) values were 0.17 mM for ATP and 0.19 mM for (R,S)-5-phosphomevalonate. The specific activity of the purified enzyme was 3.9 micromol substrate converted per minute per milligram protein. Applications to an immobilized enzyme bioreactor and to drug screening and design are discussed.

Amino Acid Sequence↗

In vitro activity and killing effect of temporin A on nosocomial isolates of Enterococcus faecalis and interactions with clinically used antibiotics.

OBJECTIVE: To study the in vitro activity of temporin A, a basic, highly hydrophobic, antimicrobial peptide amide derived from the skin of the European red frog Rana temporaria, alone and in combination with co-amoxiclav, imipenem, ciprofloxacin, linezolid and vancomycin, against 42 nosocomial isolates of Enterococcus faecalis. Fourteen of these were resistant to vancomycin. METHODS: Antimicrobial activity of temporin A was measured by MIC, MBC and time-kill studies and by the chequerboard titration method. RESULTS: All isolates were inhibited at concentrations of 1 to 16 mg/L. Combination studies carried out with E. faecalis ATCC 29212 and ATCC 51299 demonstrated synergy only when the peptide was combined with co-amoxiclav and imipenem. CONCLUSIONS: Our findings show that temporin A is active against E. faecalis and that its activity could be enhanced when it is combined with other antimicrobial agents.

Anti-Bacterial Agents↗

Comparative analysis of 18 sex pheromone plasmids from Enterococcus faecalis: detection of a new insertion element on pPD1 and implications for the evolution of this plasmid family.

A new IS element, IS1062, related to the enterococcal IS elements IS6770 and IS1252, was detected in the 3'-terminus of the surface exclusion gene, sep1, of sex pheromone plasmid pPD1 in Enterococcus faecalis. pPD1-bearing cells lack the surface exclusion function, probably as a consequence of this insertion. Analysis of pAD1 and pPD1 sequences (7.5 kb and 2.7 kb, respectively) downstream of their aggregation substance genes revealed no similarity in these DNA regions. Detailed DNA/DNA hybridization studies using DNA probes specific for various pAD1-encoded genes needed for plasmid transfer indicated that the sex pheromone plasmids have evolved by repeated recombination and insertion of diverse transposable elements which presumably account for recent acquisition of antibiotic resistances.

Amino Acid Sequence↗

Specificity of induction of glycopeptide resistance genes in Enterococcus faecalis.

Regulation of VanA- and VanB-type glycopeptide resistance in enterococci is mediated by related two-component regulatory systems (VanR-VanS and VanRB-VanSB). The transglycosylase inhibitors vancomycin, teicoplanin, and moenomycin induced synthesis of the VanX D,D-dipeptidase in a VanA-type Enterococcus faecalis harboring transposon Tn1546. Inhibitors of reactions immediately preceding (ramoplanin) or following (penicillin G and bacitracin) transglycosylation were not inducers. These results identify accumulation of membrane-bound lipid intermediate II as a potential signal for induction of VanA-type resistance. In E.faecalis BM4281 harboring a wild vanB genetic element, D,D-dipeptidase synthesis was only inducible by vancomycin. Induction of the production of the VanB ligase by vancomycin was required for growth of a vancomycin-dependent derivative of BM4281, since introduction of a plasmid coding for constitutive synthesis of the VanA ligase eliminated the requirement of glycopeptide for growth. Both vancomycin and teicoplanin were able to induce D,D-dipeptidase synthesis in BM4281 derivatives that were vancomycin and teicoplanin resistant or vancomycin and teicoplanin dependent. Acquisition of teicoplanin resistance in the latter types of strains was due to alteration in induction specificity associated with an increase in the sensitivity of the regulatory system to vancomycin. Thus, the wild VanRB-VanSB system is unable or not sensitive enough to sense teicoplanin, although mutations can lead to recognition of this antibiotic.

Anti-Bacterial Agents↗

[Therapeutic effect of cefluprenam on polymicrobial urinary tract infection associated with Enterococcus faecalis, using the infectious urolithiasis model in rats].

We examined the therapeutic effect of cefluprenam (CFLP) on the polymicrobial urinary tract infection associated with infectious stones as compared to that of ceftazidime (CAZ), using the experimental polymicrobial urinary tract infection caused by Proteus mirabilis (P. mirabilis), Pseudomonas aeruginosa (P. aeruginosa) and Enterococcus faecalis (E. faecalis). In order to form bladder stones in rats, a sterile zinc ring was implanted as a foreign body, followed by inoculating P. mirabilis E05106 transurethrelly. Thereafter, P. aeruginosa E030033 and E. faecalis 966 were inoculated according to the same way. CFLP or CAZ was administered intravenously twice a day for 5 days. The therapeutic effect was evaluated by the eradication of these bacteria from the urine, the kidney and stones, inhibition of growth of stones, and also a value of BUN. The urinary excretion rates of CFLP and CAZ was also determined (20 mg/kg). In result, CFLP significantly more effective in the eradication of P. mirabilitis, P. aeruginosa and E. faecalis from the urine, the kidney and stones than the control than the control (p < 0.05). Furthermore, CFLP significantly more effective in the eradication of P. aeruginosa from the urine and also E. facalis from the urine and stones (p < 0.05). Meanwhile, CAZ significantly more effective in the eradication of P. mirabilis from the urine, the kidney and stones and also P. aeraginosa from the kidney and stones than the control. However, CAZ did not show eradicative effect on E. faecalis. The urinary excretion rates of CFLP and CAZ at rats were 59.3% and 59.4%, respectively, within 8 hrs after administration, showing a similar excretion pattern. CFLP exhibited the prominent therapeutic effect on polymicrobial urinary tract infection associated with infectious stones caused by P. mirabilis, P. aeruginosa and E. faecalls. On the basis of these results, it has been strongly suggested that CFLP is highly beneficial in the management of intractable polymicrobial urinary tract infectious in clinic.

Animals↗

Lysed enterococcus faecalis FK-23 oral administration reveals inverse association between tuberculin responses and clinical manifestations in perennial allergic rhinitis: a pilot study.

BACKGROUND: The interest in anti-allergy immunoregulation by lactic acid bacteria (LAB) has been growing over the last few decades. There is evidence to suggest that lysed Enterococcus faecalis FK-23 (LFK), a kind of LAB preparation, could relieve the clinical symptoms of Japanese cedar pollinosis. However, little is known about how LFK plays a role in combating allergy. OBJECTIVE: The aim of this study was to clarify whether improvement of clinical manifestations is associated with enhancement of tuberculin responses in patients with allergic rhinitis treated by LFK. METHODS: One gram of LFK per day was administered orally to fifty perennial allergic rhinitis patients in an open trial that lasted 28 days. Nasal symptoms and sign scores were rated before and after administration of LFK. Tuberculin responses and peripheral blood cells were also measured before and after LFK treatment. RESULTS: Purified protein derivative (PPD) skin test diameter was 2.14 +/- 2.14 mm before LFK administration versus 7.26 +/- 4.81 mm at day 31 (p < 0.01). A significant inverse correlation was recognized between PPD skin test diameters and total nasal scores in the nasal provocation test before and after treatment (r= - 0.600, p < 0.001). Peripheral blood eosinophils were 248 +/- 149 cells/ml before LFK administration and then they significantly decreased to 76 +/- 98 cells/microl (p < 0.01). CONCLUSIONS: These finding may be interpreted as a result of improved clinical symptoms in allergic rhinitis after LFK oral treatment owing to the enhanced host's Th1-type immune responses and supression of the over-expression of Th2-dominated allergic responses.

Administration, Oral↗

Gene transfer of vancomycin and tetracycline resistances among Enterococcus faecalis during cheese and sausage fermentations.

This study assessed the frequency of transfer of two mobile genetic elements coding for virulence determinants and antibiotic resistance factors, into food associated enterococci during fermentation processes. First, the transfer of the pheromone-inducible pCF10 plasmid, carrying tetracycline resistance and aggregation substance (AS) as virulence factor, between clinical and food strains of Enterococcus faecalis, was investigated in models of cheese and fermented sausage. The experiments demonstrated that even in the absence of selective tetracycline pressure, plasmid pCF10 was transferred from E. faecalis OG1rf cells to food strain E. faecalis BF3098c and that the plasmid subsequently persisted in these environments. Very high frequency of transfer was observed in sausage (10(-3)/recipient) if compared to cheese (10(-6)) and plate mating (10(-4)). Transconjugants were subsequently verified by PCR. The second transmissible element was the plasmid harbouring the vancomycin resistance (VanA phenotype) from E. faecalis A256. The transfer of this antibiotic resistance to a food strain of E. faecalis was studied in vitro and in food models. Although the transfer of vancomycin resistance was achieved in all the environments, the highest conjugation frequencies were observed during the ripening of fermented sausages, reaching 10(-3) transconjugants/recipient cell. PCR confirmed the transfer of the VanA genotype into a food associated Enterococcus strain. This study showed that even in the absence of selective pressure, mobile genetic elements carrying antibiotic resistance and virulence determinants can be transferred at high frequency to food associated enterococci during cheese and sausage fermentation.

Animals↗

Purification and characterization of a surface-binding protein from Lactobacillus fermentum RC-14 that inhibits adhesion of Enterococcus faecalis 1131.

Lactobacilli have been shown to be important in the maintenance of the healthy urogenital flora. One strain, Lactobacillus fermentum RC-14, releases surface-active components which can inhibit adhesion of uropathogenic bacteria. Using a quantitative method for determining inhibition of adhesion, a protein with high anti-adhesive properties against Enterococcus faecalis 1131 was purified. The N-terminal sequence of the 29-kDa protein was identical to that of a collagen-binding protein from Lactobacillus reuteri NCIB 11951, and exhibited close homology with a basic surface protein from L. fermentum BR11. The results suggest that this anti-adhesive cell surface protein of Lactobacillus could protect against uropathogens by preventing their adhesion. the Federation of European Microbiological Societies.

Amino Acid Sequence↗

Distribution of four capsular serotypes of Enterococcus faecalis among clinical isolates from different geographical origins and infection sites.

BACKGROUND: Enterococci possess capsular polysaccharide antigens that are the targets of opsonic antibodies. These antibodies are potential candidates for development as immunotherapy. MATERIAL AND METHODS: The present study analyzes the distribution of four capsular serotypes within a collection of 157 isolates of Enterococcus faecalis from four countries with different sites of clinical infection. RESULTS: By using a capsular polysaccharide-specific ELISA, 42% of the isolates were grouped into one of four serogroups, and another 9% showed cross-reactivity between two serotype-specific sera. Heterogeneity of serotype distribution by both geographical origin and infection site was observed. CONCLUSION: Half of the strain collection could be typed with four serotype-specific sera. No serotype from a given country or infection site clearly predominated.

Bacterial Capsules↗

Heterologous expression of lacticin 3147 in Enterococcus faecalis: comparison of biological activity with cytolysin.

Lacticin 3147 is a broad-spectrum, two-component, lanthionine-containing bacteriocin produced by Lactococcus lactis DPC3147 which has widespread food and biomedical applications as a natural antimicrobial. Other two-component lantibiotics described to date include cytolysin and staphylococcin C55. Interestingly, cytolysin, produced by Enterococcus faecalis, has an associated haemolytic activity. The objective of this study was to compare the biological activity of lacticin 3147 with cytolysin. The lacticin 3147-encoding determinants were heterologously expressed in Ent. faecalis FA2-2, a plasmid-free strain, to generate Ent. faecalis pOM02, thereby facilitating a direct comparison with Ent. faecalis FA2-2.pAD1, a cytolysin producer. Both heterologously expressed lacticin 3147 and cytolysin exhibited a broad spectrum of activity against bacterial targets. Furthermore, enterococci expressing active lacticin 3147 did not exhibit a haemolytic activity against equine blood cells. The results thus indicate that the lacticin 3147 biosynthetic machinery can be heterologously expressed in an enterococcal background resulting in the production of the bacteriocin with no detectable haemolytic activity.

Amino Acid Sequence↗