Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 2001 Feb;45(2):480-4.
doi: 10.1128/AAC.45.2.480-484.2001.

Carbapenem resistance mechanisms in Pseudomonas aeruginosa clinical isolates

Affiliations

Carbapenem resistance mechanisms in Pseudomonas aeruginosa clinical isolates

H Pai et al. Antimicrob Agents Chemother. 2001 Feb.

Abstract

In order to define the contributions of the mechanisms for carbapenem resistance in clinical strains of Pseudomonas aeruginosa, we investigated the presence of OprD, the expressions of the MexAB-OprM and MexEF-OprN systems, and the production of the beta-lactamases for 44 clinical strains. All of the carbapenem-resistant isolates showed the loss of or decreased levels of OprD. Three strains overexpressed the MexAB-OprM efflux system by carrying mutations in mexR. These three strains had the amino acid substitution in MexR protein, Arg (CGG) --> Gln (CAG), at the position of amino acid 70. None of the isolates, however, expressed the MexEF-OprN efflux system. For the characterization of beta-lactamases, at least 13 isolates were the depressed mutants, and 12 strains produced secondary beta-lactamases. Based on the above resistance mechanisms, the MICs of carbapenem for the isolates were analyzed. The MICs of carbapenem were mostly determined by the expression of OprD. The MICs of meropenem were two- to four-fold increased for the isolates which overexpressed MexAB-OprM in the background of OprD loss. However, the elevated MICs of meropenem for some individual isolates could not be explained. These findings suggested that other resistance mechanisms would play a role in meropenem resistance in clinical isolates of P. aeruginosa.

PubMed Disclaimer

Similar articles

Cited by

References

    1. Bauerfeind A, Stemplinger I, Jungwirth R, Mangold P, Amann S, Akalin E, Ang O, Bal C, Casellas J M. Characterization of β-lactamase gene blaper-2, which encodes an extended-spectrum class A β-lactamase. Antimicrob Agents Chemother. 1996;40:616–620. - PMC - PubMed
    1. Bonfiglio G, Laksai Y, Granchino L, Amicosante G, Nicoletti G. Mechanisms of β-lactam resistance amongst Pseudomonas aeruginosa isolated in an Italian survey. J Antimicrob Chemother. 1998;42:697–702. - PubMed
    1. Bush K, Jacoby G A, Medeiros A A. A functional classification scheme for β-lactamases and its correlation with molecular structure. Antimicrob Agents Chemother. 1995;39:1211–1233. - PMC - PubMed
    1. Chen H Y, Yuan M, Livermore D M. Mechanisms of resistance to β-lactam antibiotics amongst Pseudomonas aeruginosa isolates collected in the UK in 1993. J Med Microbiol. 1995;43:300–309. - PubMed
    1. Dale J W, Godwin D, Mossakowska D, Stephenson P, Wall S. Sequence of the OXA-2 β-lactamase; comparison with other penicillin-reactive enzymes. FEBS Lett. 1985;191:39–44. - PubMed

Publication types

MeSH terms

LinkOut - more resources