Results 21 to 30 of about 905,435 (191)

Detection of metallo-β-lactamase gene blaIMP of Escherichia coli clinical isolates in Sanglah General Hospital Bali

Indonesia Journal of Biomedical Science, 2019
Background: Escherichia coli belong to the family of Enterobacteriaceae that are responsible as one of the leading cause of nosocomial infections. The emergence of Carbapenem-resistant Enterobacteriaceae presents therapeutic challenges for clinicians on choosing the correct type of antibiotics to prescribe.
Muhammad Ardi Afriansyah, Ni Nyoman Sri Budayanti, Komang Januartha Putra Pinatih   +2 more
openaire   +1 more source

The Mechanisms of Catalysis by Metallo β-Lactamases [PDF]

, 2008
Class B β-lactamases or metallo-β-lactamases (MBLs) require zinc ions to catalyse the hydrolysis of β-lactam antibiotics such as penicillins, cephalosporins, carbapenems, and cephamycins.
Michael I. Page, Page, Michael I., Badarau, Adriana, Adriana Badarau   +3 more
core   +3 more sources

Novel IMP-1 metallo-β-lactamase inhibitors can reverse meropenem resistance inEscherichia coliexpressing IMP-1 [PDF]

FEMS Microbiology Letters, 2005
IMP-1 metallo-beta-lactamase is a zinc metalloenzyme that confers antibiotic resistance to bacteria through the hydrolysis of beta-lactam antibiotics. Pathogens that express the enzyme show reduced susceptibility to carbapenems, such as meropenem and imipenem.
Joseph G, Moloughney, Janice, D Thomas, Jeffrey H, Toney   +2 more
openaire   +2 more sources

Broad antibiotic resistance profile of the subclass B3 metallo-β-lactamase GOB-1, a di-zinc enzyme. [PDF]

, 2011
peer reviewedThe metallo-β-lactamase (MBL) GOB-1 was expressed via a T7 expression system in Escherichia coli BL21(DE3). The MBL was purified to homogeneity and shown to exhibit a broad substrate profile, hydrolyzing all the tested β-lactam compounds ...
Nathalie Selevsek, Carine Bebrone, Louise E. Horsfall, Lassaux, Patricia, Benoit M. R. Liénard, Kurt M. Hoffmann, Hoffmann, Kurt, Poirel, Laurent, Michael B. Kupper, Horsfall, Louise E., Horsfall, Louise E.; id_orcid, Bebrone, Carine, Izougarhane, Youssef, Jean-Marie Frère, Lienard, Benoit M. R., Youssef Izougarhane, Selevsek, Nathalie, Kupper, Michael B., Patricia Lassaux, Kupper, Michaël, Horsfall, Louise, Laurent Poirel, Liénard, Benoit, Galleni, Moreno, Frère, Jean-Marie, Hoffmann, Kurt M., Moreno Galleni   +26 more
core   +1 more source

One origin for metallo-β-lactamase activity, or two? An investigation assessing a diverse set of reconstructed ancestral sequences based on a sample of phylogenetic trees [PDF]

, 2014
This work was supported by BBSRC (grant BB/F016778/1)Bacteria use metallo-β-lactamase enzymes to hydrolyse lactam rings found in many antibiotics, rendering them ineffective.
Barker, Daniel, Rosanna G. Alderson, John B. O. Mitchell, Daniel Barker, Alderson, Rosanna Grace, Alderson, Rosanna G, Mitchell, John B O, Mitchell, John B. O.   +7 more
core   +1 more source

Detection of bla NDM-1 Encoding Imepenemase among the Imipenem-Resistant Gram-Negative Bacilli Isolated from Various Clinical Samples at a Tertiary Care Hospital of Eastern Nepal: A Descriptive Cross-Sectional Study

International Journal of Microbiology, 2020
Background. Carbapenem resistance among Gram-negative isolates caused by the production of the metallo-β-lactamase (MBL) enzyme is being increasingly reported worldwide. One of the newly emerged metallo-β-lactamases is New Delhi metallo-β-lactamase. Data
S. Gautam, N. R. Bhattarai, K. Rai, A. Poudyal, B. Khanal   +4 more
doaj   +1 more source

Occurrence of a new metallo-β-lactamase IMP-4 carried on a conjugative plasmid inCitrobacter youngaefrom the People's Republic of China [PDF]

FEMS Microbiology Letters, 2001
During the course of an antimicrobial resistance surveillance programme in Guangzhou, the People's Republic of China, single strains of Citrobacter youngae and Pseudomonas aeruginosa were identified which were resistant to imipenem and found to carry the carbapenemase gene bla(IMP).
P M, Hawkey, J, Xiong, H, Ye, H, Li, F H, M'Zali   +4 more
openaire   +2 more sources

Biochemical characterization of the carbapenem-hydrolyzing β-lactamase AsbM1 fromAeromonas sobriaAER 14M: a member of a novel subgroup of metallo-β-lactamases [PDF]

FEMS Microbiology Letters, 1996
AsbM1, a carbapenem-hydrolyzing beta-lactamase produced by Aeromonas sobria AER 14M, was purified chromatographically, with anion exchange chromatography performed in the absence of Zn2+. The molecular mass of AsbM1 was approximately 34,000; the isoelectric point was 9.1.
Y, Yang, K, Bush
openaire   +2 more sources

Prevalence and detection of Stenotrophomonas maltophilia carrying metallo-β-lactamase blaL1 in Beijing, China [PDF]

Frontiers in Microbiology, 2014
Intrinsic β-lactam resistance in Stenotrophomonas maltophilia is caused by bla L1 and/or bla L2, a kind of metallo-β-lactamase with a broad substrate spectrum including carbapenems. A rapid and sensitive molecular method for the detection of bla L1 in clinical samples is needed to guide therapeutic treatment. In present study, we first described a loop-
Zhan eYang, Wei eLiu, Qian eCui, Qian eCui, Wen Kai Niu, Huan eLi, Xiang Na Zhao, Xiao eWei, Xue Song Wang, Si Mo Huang, De Rong Dong, Si Jing Lu, Chang Qing Bai, Yan eLi, Liu Yu Huang, Jing eYuan   +15 more
openaire   +3 more sources

First case of New Delhi metallo-β-lactamase in Klebsiella pneumoniae from Ecuador: An update for South America [PDF]

International Journal of Infectious Diseases, 2017
To describe a clinical case of Klebsiella pneumoniae harboring a New Delhi metallo-β-lactamase (NDM) plasmid in Ecuador and to present a map of reports of NDM isolates in South America.The modified Hodge test, carbapenem inactivation method, imipenem-EDTA disk method (synergy), and Rapidec Carba NP test were used to identify antibiotic resistance ...
Daniel Romero-Alvarez, Jorge Reyes, Viviana Quezada, Carolina Satán, Nelson Cevallos, Sofía Barrera, Gabriel Trueba, Luis E. Escobar, José E. Villacís   +8 more
openaire   +3 more sources