Evolution of plasmid-coded resistance to broad-spectrum cephalosporins
- 1 August 1985
- journal article
- research article
- Published by American Society for Microbiology in Antimicrobial Agents and Chemotherapy
- Vol. 28 (2), 302-307
- https://doi.org/10.1128/aac.28.2.302
Abstract
A clinical isolate of Klebsiella ozaenae with transferable resistance to broad-spectrum cephalosporins produces a .beta.-lactamase determined by plasmid pBP60. The .beta.-lactamase had the same isoelectric point as SHV-1 (7.6). From heteroduplex analysis, an extensive homology between the two bla genes could be deduced; therefore, the new .beta.-lactamase was designated SHV-2. Enzymatic studies revealed that SHV-2 was able to hydrolyze broad-spectrum cephalosporins due to an increased affinity of these compounds for the enzyme. The assumption that SHV-2 is a natural mutant of SHV-1 was strongly supported by the isolation of a laboratory mutant of SHV-1 that showed activities similar to those of SHV-2.This publication has 25 references indexed in Scilit:
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