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I Klare

Publications and source records attributed to I Klare.

6 recordsLinked to original sources
PubMed1992

Inducible carboxypeptidase activity in vancomycin-resistant enterococci.

Vancomycin was found to coinduce DD-carboxypeptidase activity, together with resistance, in eight low- or high-level glycopeptide-resistant strains of enterococci. The constitutively resistant mutant (MT10) of a low-level-resistant strain of Enterococcus faecium (D366) spontaneously expressed a level of carboxypeptidase similar to that of the induced strain D366. Pentapeptide, UDP-MurNac-pentapeptide, as well as D-alanyl-D-alanine were in vitro substrates for the carboxypeptidase which was not inhibited by penicillin. The level of vancomycin resistance correlated roughly with the level of carboxypeptidase activity. We infer from these results that the carboxypeptidase is one component of the glycopeptide resistance mechanism.

Anti-Bacterial Agents↗
PubMed1992

Overproduction of a penicillin-binding protein is not the only mechanism of penicillin resistance in Enterococcus faecium.

In 1989 and 1990, a large number of ampicillin-resistant strains of Enterococcus faecium were isolated from infected patients treated at intensive care units in Berlin, Germany. Twenty-five clinical isolates, including five different biotypes as classified by acid production from various sugars and a wide range of susceptibilities to ampicillin (MICs between 0.5 and 128 micrograms/ml), were selected for a detailed analysis of penicillin-binding proteins (PBPs). All strains contained a slowly reacting PBP with low penicillin affinity known to be present in enterococci. Overproduction of this PBP relative to susceptible isolates was noted, especially in all strains for which the MIC of ampicillin was 8 micrograms/ml, to a lesser degree in the more resistant strains, but not at all in the three highly resistant isolates for which the MIC was 128 micrograms/ml. In these three strains, this PBP appears to have a reduced affinity for beta-lactams. The results suggest that overproduction of PBP 6 correlates only with intermediate resistance levels and that higher resistance is mediated by yet another, still unknown mechanism, probably including reduction of beta-lactam affinity in one or more PBPs.

Bacterial Proteins↗
PubMed1989

[Nosocomial infections caused by multi-resistant Serratia marcescens at a university clinic--clinical aspects and drug resistance].

Serratia marcescens (S.m.) has become increasingly important as a nosocomial pathogen and displayed an increasing resistance to antimicrobial agents in the past decade. We recently studied in 1985 and 1986 an epidemic caused by multi resistant S.m. strains that involved 27 infants and 1 adult patient. 14 neonates (in most cases very low birth weight infants) in a neonatal intensive care unit developed a S.m.-septicemia and/or meningitis, 11 of them died. In a ward for young infants with congenital heart diseases 13 patients suffered a S.m. infection and one patient died in the adult intensive care unit in consequence of a S.m. septicemia.

Anti-Bacterial Agents↗
PubMedDate not supplied

Nosocomial infections due to Serratia marcescens--clinical findings, antibiotic susceptibility patterns and fine typing.

We report on nosocomial infections caused by Serratia marcescens occurring in a neonatal intensive care unit and a children's ward for cardiac intensive care. According to the plasmid pattern analysis, all isolated epidemic strains belonged to one clone. Multi-drug resistance, even to cephalosporins of the third generation and amikacin, was characteristic for all strains. Certain markers of S. marcescens (haemolysin, proteases, siderophores) which are thought to be related to virulence were studied but will require further investigation.

Anti-Bacterial Agents↗