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Journal of Antimicrobial Chemotherapy (1995) 35, 281-294
© 1995 The British Society for Antimicrobial Chemotherapy

research-article

Transferable production of PER-1 ß-lactamase in Pseudomonas aeruginosa

F. Danela, L. M. C. Halla, D. Gurb, H. E. Akalinb and D. M. Livermorea

aDepartment of Medical Microbiology, The London Hospital Medical College Turner Street, London, E1 2AD, UK bSection of Infectious Diseases, Department of Internal Medicine, Hacettepe University School of Medicine 06100 Ankara, Turkey

Received 12 April 1994; returned 21 September 1994; accepted 18 October 1994

PER-1, an extended-spectrum class A ß-lactamase, has been described only from Pseudomonas aeruginosa RNL-1, which was obtained in France in 1991. During studies on ceftazidime-resistant P. aeruginosa collected from December 1991 to July 1993 in Ankara, Turkey, we found 14 further isolates with PER-1 enzyme, as recognised by isoelectric point (pI 5·4), hydrolytic activity, gene hybridization and DNA sequence. Five of these isolates also had OXA-10 (PSE-2)-related enzymes and one hyper-produced ampC ß-lactamase, whereas eight had PER-1 enzyme alone. The last group, from four wards, appeared to be identical, giving the same DNA restriction patterns and carrying the PER-1 gene on an 8·5 kb HincII fragment. Two more producers were related but the other four were unique. In several representatives of the group of eight replicates, the PER-1 gene was shown to be encoded on a plasmid, larger than 154 kb in size, which transferred to P. aeruginosa PU21. A further isolate had the gene on an even larger conjugative plasmid. By contrast, the PER-1 gene reportedly was chromosomally-inserted in strain RNL-1. The PER-1 producers and their transconjugants were highly resistant to ceftazidime and aztreonam (MIC≥128 mg/L) but not to carbapenems or latamoxet. Piperacillin insusceptibility was marginal (MIC 8 mg/L). Clavulanate 4 mg/L, but not tazobactam 4 mg/L, reversed resistance to ceftazidime and carbenicillin. Purification of the enzyme to homogeneity was achieved by three ion exchanges and one gel filtration. We found much lower Vmax rates for aminothiazolyl cephalosporins than reported previously for PER-1 enzyme. This reflected the present assays being in 0·1 M phosphate butter pH 7·0, whereas the previous were pH-stat-regulated; concentrated phosphate reduced enzyme activity against ceftazidime, but not against cephaloridine.


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