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JAC Advance Access published online on June 12, 2003
Journal of Antimicrobial Chemotherapy, doi:10.1093/jac/dkg297
© 2003 by The British Society for Antimicrobial Chemotherapy
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© 2003 The British Society for Antimicrobial Chemotherapy

Brief report

Penicillin-binding proteins involved in high-level piperacillin resistance in Veillonella spp

Maria M. Theron 1 *, Marais N. Janse van Rensburg 1 , and Lynda J. Chalkley 2

1 Department of Medical Microbiology (G4), Faculty of Health Sciences, University of the Free State, Bloemfontein
2 Medical Research Council, Cape Town, South Africa

* Corresponding author. E-mail: gnmbml{at}med.uovs.ac.za.

Received 23 January 2003 ; revised 22 April 2003 ; accepted 23 April 2003

Abstract

Objectives: To investigate high-level piperacillin resistance in Veillonella spp. in the absence of {beta}-lactamase activity.

Methods: Penicillin-binding protein (PBP) competition studies were conducted in Veillonella strains, with piperacillin MICs ranging from 0.5 to >128 mg/L and ampicillin MICs from 0.125 to 4 mg/L. Whole cell lysates were pre-incubated with piperacillin or ampicillin and post-labelled with [3H]benzylpenicillin.

Results: PBP competition studies showed that the PBP with greatest affinity for penicillin and ampicillin had a molecular weight of ~66 kDa, and exhibited reduced binding of piperacillin in resistant strains.

Conclusions: This unusual focusing of different penicillins on one PBP may be the cause of selective mutants resulting from piperacillin MICs > 128 mg/L. In the absence of {beta}-lactamases, alterations in penicillin-binding were seen to be major contributors to high-level piperacillin resistance development.

Keywords: anaerobic bacteria, resistance, penicillins, Gram-negative bacteria, {beta}-lactams
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