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PubMed1989

In vitro synergism between daptomycin and fosfomycin against Enterococcus faecalis isolates with high-level gentamicin resistance.

Daptomycin and fosfomycin are two agents which inhibit different steps in peptidoglycan synthesis. We studied the in vitro activities of these drugs, alone and in combination, by time-kill techniques against 21 clinical isolates of Enterococcus (Streptococcus) faecalis demonstrating high-level resistance to gentamicin. Combinations of fosfomycin and daptomycin exhibited synergistic bactericidal activity (100-fold decrease in CFU per milliliter at 24 h compared with daptomycin alone) against all strains (mean +/- standard deviation of increment in killing = 2.7 +/- 0.7 log10 CFU/ml). In a subgroup of strains against which daptomycin (5 micrograms/ml) alone was bactericidal (greater than 3 log10 killing), synergistic activity was demonstrable only when the concentration of daptomycin was lowered to 0.25 to 0.5 microgram/ml. A 50% dilution of human serum diminished the bactericidal activity of daptomycin alone at 24 h but did not affect killing observed with the daptomycin-fosfomycin combination. The inhibition of peptidoglycan synthesis by the combination was greater than the inhibition observed with either drug alone. The combination of daptomycin and fosfomycin exhibited consistent synergistic bactericidal activity against strains of E. faecalis possessing high-level resistance to gentamicin. This synergism may be the result of sequential inhibition of early steps in peptidoglycan synthesis.

Anti-Bacterial Agents↗
PubMed1988

Regulation of the pAD1 sex pheromone response in Enterococcus faecalis: construction and characterization of lacZ transcriptional fusions in a key control region of the plasmid.

Strains carrying the Enterococcus (formerly Streptococcus) faecalis plasmid pAD1 responded to exogenous sex pheromone by inducing a number of gene products which facilitated mating. A 7-kilobase region of pAD1 was identified which contained genes that are important for the regulation of this response. Using the transposon Tn917-lac delivery vector pTV32Ts, we generated a number of fusions that allowed us to examine transcription in this region. At least three transcriptional units were identified by grouping fusions by their phenotype, direction of transcription, and response to pheromone. Transcription from one set of fusions was sensitive to the presence of pheromone. Analysis of the patterns of protein production previously shown to be induced in the presence of pheromone provided more information on the function of the genes of interest. We postulate the existence of two negative regulatory proteins that act coordinately to repress the pheromone response, one of which may be involved in sensing or transmitting the pheromone signal, and at least one positive regulatory protein whose synthesis is dependent on the presence of pheromone. In addition, the isolation of a relatively small deletion mutant capable of producing cAD1. the pheromone specific for pAD1-containing cells, indicates that a factor(s) that is important for the shutdown of endogenous pheromone is also present in this region.

Bacterial Proteins↗
PubMed1990

Amino acid sequence of pheromone-inducible surface protein in Enterococcus faecalis, that is encoded on the conjugative plasmid pPD1.

The major pheromone-inducible protein, PD78, believed to contribute to bacterial conjugation, was purified from Enterococcus (formerly Streptococcus) faecalis cells containing the plasmid pPD1. A cloned EcoRI-BglII 3.6-kbp fragment of the plasmid pAM351(pPdl::Tn916) contained an open reading frame corresponding to 467 amino acid residues representing PD78. In a central region of the deduced protein, there is a repeated sequence of X-X-Pro that is repeated 15 times. This is analogous to the Gln-Gln-Pro repeat in the C-terminal region of TraD product encoded on the R100 plasmid in Escherichia coli.

Amino Acid Sequence↗
PubMed1990

Amino acid sequence of pheromone-inducible surface protein in Enterococcus faecalis, that is encoded on the conjugative plasmid pPD1.

The major pheromone-inducible protein, PD78, believed to contribute to bacterial conjugation, was purified from Enterococcus (formerly Streptococcus) faecalis cells containing the plasmid pPD1. A cloned EcoRI-BglII 3.6-kbp fragment of the plasmid pAM351 (pPD1::Tn916) contained an open reading frame corresponding to 467 amino acid residues representing PD78. In a central region of the deduced protein, there is a repeated sequence of X-X-Pro that is repeated 15 times. This is analogous to the Gln-Gln-Pro repeat in the C-terminal region of TraD product encoded on the R100 plasmid in Escherichia coli.

Amino Acid Sequence↗
PubMed2003

Outbreak of infection with high-level gentamicin-resistant Enterococcus faecalis (HLGRE) in a Norwegian hospital.

OBJECTIVES: To examine and characterize a suspected outbreak of high-level gentamicin-resistant Enterococcus (HLGRE) infection. METHODS: Eighty-nine patients with clinical infection diagnosed during hospital stay or within 30 days after discharge in the period from June 1995 to 31 December 1999 were included in the study. One control patient was assigned for each HLGRE patient according to localization in the hospital (same ward), time of admission (+/-3 months), and age (+/-10 years). Unadjusted risk analysis and multivariate logistic regression analysis were performed. Sixty-nine HLGRE strains were subjected to PCR amplification of the genes coding for aminoglycoside-3'-O-phosphoryltransferase-III (APH(3')-III) and aminoglycoside-6'-N-acetyltransferase/2"-O-phosphoryltransferase-III (AAC(6')/APH(2")). RESULTS: The gene aacA/aphD, associated with HLGRE, was detected by PCR in all isolates, and the gene aphA3, associated with high-level streptomycin, kanamycin and amikacin resistance, was detected in 56 of the 69 isolates. None of the 69 isolates was resistant to glycopeptides or ampicillin. Resistance to ciprofloxacin was found in 57 (82.6%). Pulsed-field gel electrophoresis analysis revealed 12 different genotypes, among which two major clusters dominated. CONCLUSIONS: Both clonal expansion and the emergence of unique strains contributed to the increased number of infections caused by HLGRE. Urinary catheterization, duration of hospital stay and antibiotic therapy were significant risk factors for HLGRE infection.

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