title: Beta-lactamase-directed barrier for penicillins of Escherichia coli carrying R plasmids.
abstract: Strains of Escherichia coli and Salmonella typhimurium carrying R plasmids, which were obtained from ampicillin-resistant clinical isolates of E. coli and Klebsiella spp. and specified either the type IIIa (TEM-type) or type Va (oxacillin-hydrolyzing) beta-lactamase, are resistant not only to ampicillin but also to carbenicillin and sulbenicillin. The latter two derivatives, however, are poorly hydrolyzed in vitro by the beta-lactamases. Although values of K(m) of the enzymes are lower for sulbenicillin and carbenicillin than for ampicillin, the ratios of V(max) to K(m) for sulbenicillin and carbenicillin are not high enough to explain the high resistance in E. coli bearing the R plasmid. Two mutants of the plasmids conferring a temperature-sensitive ampicillin resistance were induced by nitrosoguanidine treatment. It was confirmed that E. coli CSH2, harboring the mutant plasmid, produces a temperature-sensitive beta-lactamase and is resistant only at low temperatures (below 33 degrees C), but not at 42 degrees C, to ampicillin, sulbenicillin, and carbenicillin simultaneously. It is thus concluded that beta-lactamase itself is responsible for the mechanism of resistance not only to ampicillin but also to sulbenicillin and carbenicillin, even though the enzyme as determined in cell-free extracts hydrolyzes the latter two drugs poorly. An unknown barrier for sulbenicillin and carbenicillin directed by beta-lactamase in E. coli strains carrying R (bla) plasmids is postulated.
mesh_terms: D004926:Escherichia coli / Q000187:drug effects* / Q000201:enzymology; D010403:Penicillin Resistance; D010405:Penicillinase / Q000378:metabolism*; D010406:Penicillins / Q000494:pharmacology*; D011815:R Factors
chemical_list: D010406:Penicillins; D010405:Penicillinase