Identification and Characterization of Carbapenem Hydrolysing β-lactamase – KPC among Enterobacteriaceae: A report from North India
Objective: The serine carbapenemase KPC (Klebsiella pneumoniae carbapenemase) has emerged as a beta-lactamase capable of inactivating carbapenem antibiotics. The emergence of carbapenem-resistant enterobacteria is therefore worrisome, since consequently the antimicrobial treatment options are very r...
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Manipal College of Medical Sciences, Pokhara
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doaj-463136eb787b42d582a5253ab913b8ee2020-11-25T03:00:04ZengManipal College of Medical Sciences, PokharaAsian Journal of Medical Sciences2467-91002091-05762013-02-01321115https://doi.org/10.3126/ajms.v3i2.5087Identification and Characterization of Carbapenem Hydrolysing β-lactamase – KPC among Enterobacteriaceae: A report from North IndiaSupriya Upadhyay 0Department of Microbiology, Institute of Medical Sciences, Banaras Hindu University, VaranasiObjective: The serine carbapenemase KPC (Klebsiella pneumoniae carbapenemase) has emerged as a beta-lactamase capable of inactivating carbapenem antibiotics. The emergence of carbapenem-resistant enterobacteria is therefore worrisome, since consequently the antimicrobial treatment options are very restricted. In the present study we have reported the presence of KPC ?-lactamase producing enterobacterial isolates from a tertiary referral hospital in north India. Methods: The isolates were subjected to phenotypic confirmatory test by boronic acid and clavulanic acid inhibition and presence of carbapenemase activity. They were further tested for PCR detection of blaKPC and the associated genetic component. Results: Three enterobacterial isolates were found to be phenotypically similar to that of KPC enzyme and genotypically showing positive results with primers specific for blaKPC gene were found to be located on integron. Conclusion: The findings indicate the need for continuous surveillance of this resistant determinant in this part of the world.https://www.nepjol.info/index.php/AJMS/article/view/5087serine carbapenemaseskpcintegron |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Supriya Upadhyay |
spellingShingle |
Supriya Upadhyay Identification and Characterization of Carbapenem Hydrolysing β-lactamase – KPC among Enterobacteriaceae: A report from North India Asian Journal of Medical Sciences serine carbapenemases kpc integron |
author_facet |
Supriya Upadhyay |
author_sort |
Supriya Upadhyay |
title |
Identification and Characterization of Carbapenem Hydrolysing β-lactamase – KPC among Enterobacteriaceae: A report from North India |
title_short |
Identification and Characterization of Carbapenem Hydrolysing β-lactamase – KPC among Enterobacteriaceae: A report from North India |
title_full |
Identification and Characterization of Carbapenem Hydrolysing β-lactamase – KPC among Enterobacteriaceae: A report from North India |
title_fullStr |
Identification and Characterization of Carbapenem Hydrolysing β-lactamase – KPC among Enterobacteriaceae: A report from North India |
title_full_unstemmed |
Identification and Characterization of Carbapenem Hydrolysing β-lactamase – KPC among Enterobacteriaceae: A report from North India |
title_sort |
identification and characterization of carbapenem hydrolysing β-lactamase – kpc among enterobacteriaceae: a report from north india |
publisher |
Manipal College of Medical Sciences, Pokhara |
series |
Asian Journal of Medical Sciences |
issn |
2467-9100 2091-0576 |
publishDate |
2013-02-01 |
description |
Objective: The serine carbapenemase KPC (Klebsiella pneumoniae carbapenemase) has emerged as a beta-lactamase capable of inactivating carbapenem antibiotics. The emergence of carbapenem-resistant enterobacteria is therefore worrisome, since consequently the antimicrobial treatment options are very restricted. In the present study we have reported the presence of KPC ?-lactamase producing enterobacterial isolates from a tertiary referral hospital in north India.
Methods: The isolates were subjected to phenotypic confirmatory test by boronic acid and clavulanic acid inhibition and presence of carbapenemase activity. They were further tested for PCR detection of blaKPC and the associated genetic component.
Results: Three enterobacterial isolates were found to be phenotypically similar to that of KPC enzyme and genotypically showing positive results with primers specific for blaKPC gene were found to be located on integron.
Conclusion: The findings indicate the need for continuous surveillance of this resistant determinant in this part of the world. |
topic |
serine carbapenemases kpc integron |
url |
https://www.nepjol.info/index.php/AJMS/article/view/5087 |
work_keys_str_mv |
AT supriyaupadhyay identificationandcharacterizationofcarbapenemhydrolysingbetalactamasekpcamongenterobacteriaceaeareportfromnorthindia |
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