Effect of drug treatment options on the mobility and expression of blaKPC

Roth, Amanda L.; Lister, Philip; Hanson, Nancy D.

doi:10.1093/jac/dkt280

Cited by 5 publications

(2 citation statements)

References 26 publications

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“…Another study from the same group has demonstrated an increase in KPC expression when exposed to sub, MIC and suprainhibitory concentrations of antibiotic, even non-βlactam drugs. Their findings still suggest that strain and genera have a great influence in KPC expression [32]. Therapeutic failure with carbapenems against KPC producers with low MICs has been reported, corroborating the idea of induced expression [33].…”

Section: Discussionmentioning

confidence: 76%

High-performance method to detection of Klebsiella pneumoniae Carbapenemase in Enterobacterales by LC-MS/MS

et al. 2020

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Carbapenem-resistant Enterobacterales (CREs) have been recognized as an important threat to global health. CRE cause the majority of the difficult-to-treat infections in health-care settings and are associated with high mortality. Klebsiella pneumoniae carbapenemase (KPC)-producing CREs, in particular Klebsiella pneumoniae, are globally disseminated and responsible for a large number of outbreaks. Development of rapid methods for KPC detection can provide great clinical and epidemiological benefits to prevent KPC dissemination. The aim of this study was to standardize and validate a LC-MS/MS method to detect KPC. This method was also tested against a broad variety of species, including CRE with other carbapenemase genes and the recently reported mcr-1. For validation, 111 isolates with reduced susceptibility to carbapenems were selected (49 KPC-positive and 62 KPC-negative). The presence of four tryptic peptides related to the KPC enzyme was evaluated, and the identification of at least two of them classified the isolate as "KPC-positive." The LTLGSALAAPQR and LALEGLGVNGQ peptides were both detected in 47 of 49 isolates with the bla KPC gene. The other two peptides, GFLAAAVLAR and APIVLAVYTR, were detected in 46 and 19 isolates with the bla KPC gene, respectively. The method correctly classified 47 of 49 KPC-positive and all KPCnegative isolates yielding 96.07% of sensitivity and 100% of specificity. In conclusion, our results demonstrate that the KPC peptide markers were robustly detected by the method which presented high sensitivity and full specificity and therefore can be used as a reliable method to identify this resistance mechanism.

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Section: Discussionmentioning

confidence: 76%

High-performance method to detection of Klebsiella pneumoniae Carbapenemase in Enterobacterales by LC-MS/MS

et al. 2020

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“…This situation would not normally be expected. However, Roth et al demonstrated that, due to uncertain modifications in bla KPC expression, an increase in MIC for some antibiotics can occur in some species in the presence of subinhibitory concentrations ( 30 ). However, the exact mechanism that induces this situation is still unclear.…”

Section: Discussionmentioning

confidence: 99%

A Rapid and Easy Method of MALDI Biotyper Antibiotic Susceptibility Test Rapid Assay To Provide Early Meropenem Susceptibility Profile in Enterobacterales

et al. 2023

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Detection of KPC enzyme by MALDI-TOF MS from bacteria impregnated in filter paper

Wilhelm,

Moreira,

Carneiro

et al. 2024

Journal of Microbiological Methods

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Effect of drug treatment options on the mobility and expression of blaKPC

Abstract: While the changes in bla(KPC) RNA expression are subtle, the different responses observed suggest both strain- and genera-specific variations in response to different antibiotic treatments.

Cited by 5 publications

References 26 publications

High-performance method to detection of Klebsiella pneumoniae Carbapenemase in Enterobacterales by LC-MS/MS

High-performance method to detection of Klebsiella pneumoniae Carbapenemase in Enterobacterales by LC-MS/MS

A Rapid and Easy Method of MALDI Biotyper Antibiotic Susceptibility Test Rapid Assay To Provide Early Meropenem Susceptibility Profile in Enterobacterales

Detection of KPC enzyme by MALDI-TOF MS from bacteria impregnated in filter paper

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