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PubMed1973

Newer antibiotics.

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Anti-Bacterial Agents↗
PubMed1995

Saturation of penicillin-binding protein 1 by beta-lactam antibiotics in growing cells of Bacillus licheniformis.

With the help of a new highly sensitive method allowing the quantification of free penicillin-binding proteins (PBPs) and of an integrated mathematical model, the progressive saturation of PBP1 by various beta-lactam antibiotics in growing cells of Bacillus licheniformis was studied. Although the results confirmed PBP1 as a major lethal target for these compounds, they also underlined several weaknesses in our present understanding of this phenomenon. In growing cells, but not in resting cells, the penicillin target(s) appeared to be somewhat protected from the action of the inactivators. In vitro experiments indicated that amino acids, peptides and depsipeptides mimicking the peptide moiety of the nascent peptidoglycan significantly interfered with the acylation of PBP1 by the antibiotics. In addition, the level of PBP1 saturation at antibiotic concentrations corresponding to the minimum inhibitory concentrations was not constant, suggesting that additional, presently undiscovered, factors might be necessary to account for the experimental observations.

Acylation↗
PubMed1986

Inhibition of beta-lactam antibiotics at two different times in the cell cycle of Streptococcus faecium ATCC 9790.

Treatment of Streptococcus faecium ATCC 9790 with sublytic concentrations of beta-lactam antibiotics revealed two different division blocks in the cell division cycle. One block, induced by N-formimidoyl thienamycin and methicillin, occurred before the completion of chromosome replication, whereas the other, induced by cefoxitin and cephalothin, took place later in the cycle. In addition, these antibiotics gave rise to distinct morphological forms; the antibiotics acting at the earlier block point produced mainly "dumbbells," whereas those affecting the later time formed "lemons." When used in combination N-formimidoyl thienamycin and cefoxitin exerted synergistic killing on this strain. These data suggest that beta-lactam antibiotics have at least two sites of action in S. faecium.

Anti-Bacterial Agents↗
PubMed1986

Enhancement of fluorescence development of end products by use of a fluorescence developer solution in a rapid and sensitive fluorescent spot test for specific detection of microbial beta-lactamases.

A fluorescent spot test method for specific detection of microbial beta-lactamases as previously published (K. C. S. Chen, J. S. Knapp, and K. K. Holmes, J. Clin. Microbiol. 19:818-825, 1984) was improved by the use of a fluorescence developer solution. The fluorescence developer solution used in this study consisted of 0.78 M sodium tartrate buffer containing 12% formaldehyde at a final pH of 4.5. An addition of 1 volume of fluorescence developer solution to 5 volumes of ampicillin or cephalex substrate solution incubated with beta-lactamase-producing organisms, followed by heating the mixture at 45 degrees C for 10 min resulted in enhancement of fluorescence of the end products of beta-lactamase activity. This provides a more sensitive assay for microbial beta-lactamases and offers the potential for direct detection of beta-lactamases in clinical specimens.

Amidohydrolases↗
PubMed1980

The cephalosporins: activity and clinical use.

The cephalosporin antibiotics have been employed with increasing frequency since their introduction into clinical practice in the early 1960s. With the exception of cephaloridine, cephalosporin compounds are not associated with the production of significant untoward effects. The availability of newer cephalosporins, both oral and parenteral, with enhanced antibacterial activity, has expanded the clinical indications for administration of these antibiotics.

Cefaclor↗
PubMed1976

The in vitro spectrum of the cephalosporins.

The cephalosporins may currently be classified according to their relative susceptibility to beta-lactamases. Cefoxitin, cefamandole, cefatrizine, and cephanone are relatively resistant to the gram-negative beta-lactamases, whereas cephalothin, cefamandole, and cefoxitin are resistant to staphylococcal beta-lactamase. Although the inhibitory activity of cephalothin is representative of that of cephaloridine, cephalexin, cefazolin, cephapirin, cephacetrile, and cephradine, there are significant differences between its activity and that of cefoxitin, cefamandole, and cefatrizine, especially against Enterobacter, Serratia, indole-positive Proteeae, Bacteroides fragilis, and ampicillin-resistant Haemophilus influenzae.

Bacteria↗