Low-frequency transduction of imipenem resistance and high-frequency transduction of ceftazidime and aztreonam resistance by the bacteriophage AP-151isolated from a Pseudomonas aeruginosa strain

Citation
J. Blahova et al., Low-frequency transduction of imipenem resistance and high-frequency transduction of ceftazidime and aztreonam resistance by the bacteriophage AP-151isolated from a Pseudomonas aeruginosa strain, J CHEMOTHER, 12(6), 2000, pp. 482-486
Citations number
8
Categorie Soggetti
Pharmacology
Journal title
JOURNAL OF CHEMOTHERAPY
ISSN journal
1120009X → ACNP
Volume
12
Issue
6
Year of publication
2000
Pages
482 - 486
Database
ISI
SICI code
1120-009X(200012)12:6<482:LTOIRA>2.0.ZU;2-2
Abstract
Bacteriophage AP-151, isolated from a multidrug resistant Pseudomonas aerug inosa strain, was found to transduce antibiotic resistance determinants to recipient strains of P. aeruginosa. Resistance to cefotaxime, ceftazidime, aztreonam, imipenem and meropenem was transduced as a block, at different f requencies, to two P, aeruginosa strains. Resistance was two logarithms hig her (in the range 10(-5)) for cefotaxime, ceftazidime or aztreonam than for imipenem in recipient strain PAO-1670. The frequency of transduced imipene m resistance was also lower in recipient strain ML-1008, This phenomenon re flects the difference in the lytic activity of AP-151 in both strains, as t he titer of the AP-151 phage in the PAO strain was found to be restricted t o 10(-4)-10(-5) in contrast to the titer of the same phage in the ML strain which was 10(-10). The limited lytic activity in the PAO recipient strain was correlated with higher transducing activity. It can be concluded that s ome wild-type bacteriophages of P, aeruginosa might have highly individual relations between lytic and transducing activity in various potential recip ient nosocomial strains of P, aeruginosa, The nature of resistance to cefta zidime and imipenem was studied using clavulanate and EDTA as inhibitors of individual class of beta-lactamases, indicating the presence of extended-s pectrum beta-lactamase and a metallo-beta-lactamase in this isolate.