PubMed Health⌕ Search
Home/Archive/PubMed

PubMed · 3527637

Antimicrobial update.

R A Prince
View original source ↗Export metadata ↓

Abstract

New and soon-to-be introduced antimicrobials are reviewed and compared with agents already in use to determine possible therapeutic and/or cost advantages. Drugs discussed are amdinocillin, ticarcillin/clavulanic acid, ceftriaxone, ceftazidime, imipenem/cilastatin, aztreonam, and quinolones.

Explore related subjects

AmdinocillinAnti-Bacterial AgentsAztreonamBacteriaCeftazidimeCeftriaxoneCilastatinClavulanic AcidClavulanic AcidsCyclopropanesDipeptidasesHumansImipenemThienamycinsTicarcillinJournal Article

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

R A Prince. Antimicrobial update.. https://doi.org/10.1177/106002808602000716

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

PubMed1992

A murein hydrolase is the specific target of bulgecin in Escherichia coli.

A deletion in the structural gene for the soluble lytic transglycosylase, the predominant murein hydrolase in the soluble fraction of Escherichia coli, has been constructed. The mutant grows normally but exhibits increased sensitivity toward mecillinam, a beta-lactam specific for penicillin-binding protein 2. In the presence of furazlocillin or other beta-lactams with a specificity for penicillin-binding protein 3 which normally cause filamentation, bulges were formed prior to rapid bacteriolysis. Similar morphological alterations are known to develop in wild type E. coli cells when furazlocillin is combined with bulgecin, an antibiotic of unusual glucosaminyl structure. It turned out that bulgecin specifically inhibits the Sl-transglycosylase in a noncompetitive manner. Since bulgecin shows some structural analogy to the murein subunits we postulate that the soluble lytic transglycosylase, in addition to its active site, has a recognition site for specific murein structures. The possibility of an allosteric modulation of the activity of the enzyme by changes in the structure of the murein sacculus is discussed.

Amdinocillin↗
PubMed1992

Leucine and serine induce mecillinam resistance in Escherichia coli.

We have previously shown that resistance to the beta-lactam mecillinam in Escherichia coli can be brought about by a high ppGpp pool, as observed under conditions of partial amino acid starvation and RelA-dependent induction of the stringent response. We show here that our E. coli wild-type strain, which is sensitive to mecillinam on minimal glucose plates, becomes resistant in the presence of L-leucine or L-serine (or cysteine, which inactivates the antibiotic). The resistance, which is not a transient effect and does not depend on the physiological state of the cells when plated, is specific for mecillinam and is reversed by the presence of isoleucine and valine in the medium. At least in the case of serine, the resistance is RelA-dependent. We conclude that the presence of leucine and serine in the growth medium cause partial starvation for isoleucine/valine, leading to induction of the stringent response and concomitant resistance to mecillinam.

Amdinocillin↗