Regional Spread of
            <i>Pseudomonas aeruginosa</i>
            ST357 Producing IMP-7 Metallo-β-Lactamase in Central Europe

Hrabák, Jaroslav; Červená, Dana; Izdebski, Radosław; Duljasz, Wojciech; Gniadkowski, Marek; Fridrichová, Marta; Urbášková, P; Žemličková, Helena

doi:10.1128/jcm.00684-10

Cited by 43 publications

(33 citation statements)

References 19 publications

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“…To date, 5 P. aeruginosa ST357 isolates from France, Nigeria, Poland, Senegal, and Singapore have been registered on the PubMLST website (http: //pubmlst.org/paeruginosa/). Regional spread of P. aeruginosa ST357 producing IMP-7 has been reported in central Europe (27). The two isolates of NCGM1496 and NCGM1663 from different regions belonged to ST357, indicating that ST357 isolates will exist widely in Japan, although PFGE analysis revealed that the isolates were not very close to each other (with 66.7% similarity).…”

Section: Discussionmentioning

confidence: 94%

IMP-43 and IMP-44 Metallo-β-Lactamases with Increased Carbapenemase Activities in Multidrug-Resistant Pseudomonas aeruginosa

Tada

Miyoshi‐Akiyama

Shimada

et al. 2013

Antimicrob Agents Chemother

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bTwo novel IMP-type metallo-␤-lactamase variants, IMP-43 and IMP-44, were identified in multidrug-resistant Pseudomonas aeruginosa isolates obtained in medical settings in Japan. Analysis of their predicted amino acid sequences revealed that IMP-43 had an amino acid substitution (Val67Phe) compared with IMP-7 and that IMP-44 had two substitutions (Val67Phe and Phe87Ser) compared with IMP-11. The amino acid residue at position 67 is located at the end of a loop close to the active site, consisting of residues 60 to 66 in IMP-1, and the amino acid residue at position 87 forms a hydrophobic patch close to the active site with other amino acids. An Escherichia coli strain expressing bla IMP-43 was more resistant to doripenem and meropenem but not to imipenem than one expressing bla IMP-7 . An E. coli strain expressing bla IMP-44 was more resistant to doripenem, imipenem and meropenem than one expressing bla IMP-11 . IMP-43 had more efficient catalytic activities against all three carbapenems than IMP-7, indicating that the Val67Phe substitution contributed to increased catalytic activities against carbapenems. IMP-44 had more efficient catalytic activities against all carbapenems tested than IMP-11, as well as increased activities compared with IMP-43, indicating that both the Val67Phe and Phe87Ser substitutions contributed to increased catalytic activities against carbapenems.

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Section: Discussionmentioning

confidence: 94%

IMP-43 and IMP-44 Metallo-β-Lactamases with Increased Carbapenemase Activities in Multidrug-Resistant Pseudomonas aeruginosa

Tada

Miyoshi‐Akiyama

Shimada

et al. 2013

Antimicrob Agents Chemother

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“…Well-typed bacterial carbapenem-nonsusceptible isolates from the collection of the Department of Microbiology of the Faculty of Medicine and University Hospital in Plzen were used for the study (1,2,8,9). Additionally, clinical isolates susceptible to carbapenems were included (Table 1).…”

Section: Methodsmentioning

confidence: 99%

Carbapenemase Activity Detection by Matrix-Assisted Laser Desorption Ionization-Time of Flight Mass Spectrometry

et al. 2011

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Matrix-assisted laser desorption ionization-time of flight (MALDI-TOF) mass spectrometry is used for the determination of molecular weights of different chemical compounds. We describe here the use of MALDI-TOF mass spectrometry to detect a carbapenem antibiotic, meropenem, and its degradation products. Buffered meropenem solution (0.1 mM Tris-HCl, pH 6.8) was mixed with an overnight culture of bacteria. After 3-h incubation, the reaction mixture was centrifuged, and the supernatant was analyzed by MALDI-TOF mass spectrometry. The presence or absence of peaks representing meropenem and its sodium salts was crucial. The average turnaround time of this test, considering the use of overnight culture, is 4 h. We validated this method for the detection of resistance to carbapenems in Enterobacteriaceae and Pseudomonas aeruginosa mediated by carbapenemase production. A total of 124 strains, including 30 carbapenemase-producing strains, were used in the study. The sensitivity of this method is 96.67%, with a specificity of 97.87%. Our results demonstrate the ability of this method to routinely detect carbapenemases in Enterobacteriaceae and Pseudomonas spp. in laboratories. This assay is comparable with a labor-intensive imipenem-hydrolyzing spectrophotometric assay that is a reference method for the detection of carbapenemase. As demonstrated here, MALDI-TOF mass spectrometry may be used in microbiological laboratories not only for microbial identification but also for other applications, such as studies of mechanisms of antibiotic resistance.

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“…The IMP-13-producing P. aeruginosa isolate belonged to a new ST, ST1982. This ST is closely related to the ST357 clone that was previously described to be associated with the regional dissemination of IMP-7 in central Europe (15), but it is not related to ST621, an ST currently spreading worldwide (16). The VIM-2-producing P. aeruginosa isolates belonged to a new ST, ST2026.…”

mentioning

confidence: 96%

Dissemination of Carbapenemase-Producing Enterobacteriaceae and Pseudomonas aeruginosa in Romania

Dortet

Flonta²,

Boudehen

et al. 2015

Antimicrob Agents Chemother

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dFifteen carbapenemase-producing Enterobacteriaceae isolates and 12 carbapenemase-producing Pseudomonas aeruginosa isolates were recovered from patients hospitalized between August 2011 and March 2013 at the Hospital of Infectious Disease, ClujNapoca, Romania. One KPC-, nine NDM-1-, four OXA-48-, and one VIM-4-producing Enterobacteriaceae isolates along with 11 VIM-2-producing and one IMP-13-producing P. aeruginosa isolates were recovered from clinical samples. All carbapenemase genes were located on self-conjugative plasmids and were associated with other resistance determinants, including extendedspectrum ␤-lactamases and RmtC methylases.

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Regional Spread of Pseudomonas aeruginosa ST357 Producing IMP-7 Metallo-β-Lactamase in Central Europe

Cited by 43 publications

References 19 publications

IMP-43 and IMP-44 Metallo-β-Lactamases with Increased Carbapenemase Activities in Multidrug-Resistant Pseudomonas aeruginosa

IMP-43 and IMP-44 Metallo-β-Lactamases with Increased Carbapenemase Activities in Multidrug-Resistant Pseudomonas aeruginosa

Carbapenemase Activity Detection by Matrix-Assisted Laser Desorption Ionization-Time of Flight Mass Spectrometry

Dissemination of Carbapenemase-Producing Enterobacteriaceae and Pseudomonas aeruginosa in Romania

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