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. 1985 Aug;28(2):302–307. doi: 10.1128/aac.28.2.302

Evolution of plasmid-coded resistance to broad-spectrum cephalosporins.

C Kliebe, B A Nies, J F Meyer, R M Tolxdorff-Neutzling, B Wiedemann
PMCID: PMC180236  PMID: 3879659

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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