Extended broad spectrum β-lactamase in Klebsiella pneumoniae including resistance to cephamycins

Abstract

A plasmid-encoded β-lactamase conferring extended broad spectrum resistance including cephamycins was identified in a Klebsiella pneumoniae strain isolated from a patient's wound. Strains harbouring the plasmid pMVP-1 were resistant to penicillins, cephalosporins of all generations (parenteral and new oral compounds) cephamycins, aztreonam, tetracycline, chloramphenicol, sulfonamides and to all aminoglycosides modified by AAC-(6)-I-transferase. β-lactams still active against these strains were temocillin, ceftazidime, cefpirome, carumonam and the carbapenems imipenem and meropenem. The new cephamycinase (CMY-1) was more strongly inhibited by sulbactam in the majority of combinations than by clavulanic acid or tazobactam. MICs of ceftazidime and carumonam were not reduced by inhibitors in the wild type and the transconjugant. A transferable plasmid (pMVP-1) of about 9.6 × 107 dalton was demonstrated by gel-electrophoresis. In the wild type and the transconjugant a β-lactamase with an isoelectric point of 8.0 was identified. This enzyme CMY-1 is different from the other extended broad spectrum β-lactamases (TEM-3 to TEM-10, SHV-2 to SHV-5). The incidence of this enzyme may be underestimated, since resistance to cephamycins in Klebsiella and Escherichia coli has so far been regarded as almost exclusively chromosomally encoded and sensitivity of CMY-1 to clavulanic acid is low. Therefore, screening for CMY-1 beta-lactamases by the usual double disk test including clavulanic acid is not sensitive enough to detect CMY-1 producers. Sulbactam (e. g. in combination with ampicillin) disks and a cephamycin should therefore be used as well when screening for super extended broad spectrum (SEBS-) beta-lactamases. © 1989 MMV Medizin Verlag GmbH München.