Results 1 to 10 of about 14,068 (191)

A Novel Single-Tube Eicosaplex/Octaplex PCR System for the Detection of Extended-Spectrum β-Lactamases, Plasmid-Mediated AmpC β-Lactamases, and Integrons in Gram-Negative Bacteria [PDF]

Antibiotics, 2023
We developed two multiplex polymerase chain reactions (PCRs) for the detection of extended-spectrum β-lactamases (ESBLs), plasmid-mediated AmpC β-lactamases, aac(6′)-Ib gene, and integrase genes (intI1, intI2, and intI3) in class 1, 2, and 3 integrons in
Ahmed M. Soliman, Hirofumi Nariya, Daiki Tanaka, Toshi Shimamoto, Tadashi Shimamoto   +4 more
doaj   +2 more sources

AmpC β-lactamases: A key to antibiotic resistance in ESKAPE pathogensGithub [PDF]

The Cell Surface
Background: AmpC β-lactamases (blaAmpC) are essential drivers of antimicrobial resistance (AMR) in ESKAPE pathogens, bacteria that cause hospital-acquired infections.
Deeksha Pandey, Isha Gupta, Dinesh Gupta
doaj   +2 more sources

Rapid Detection of Extended-Spectrum β-Lactamases (ESBL) and AmpC β-Lactamases in Enterobacterales: Development of a Screening Panel Using the MALDI-TOF MS-Based Direct-on-Target Microdroplet Growth Assay [PDF]

Frontiers in Microbiology, 2019
Introduction: Antibiotic resistant bacteria are a growing concern worldwide. Extended-spectrum β-lactamases (ESBL) represent the most common resistance mechanism of Gram-negative bacteria against β-lactams, underlining the need for adequate diagnostic ...
Carlos L. Correa-Martínez, Evgeny A. Idelevich, Katrin Sparbier, Markus Kostrzewa, Karsten Becker   +4 more
doaj   +2 more sources

AmpC β-Lactamase-Producing Microorganisms in South American Hospitals: A Meta-Regression Analysis, Meta-Analysis, and Review of Prevalence [PDF]

Tropical Medicine and Infectious Disease
AmpC β-lactamases are class C enzymes that hydrolyze penicillins, cephalosporins, and monobactams. The WHO recently classified third-generation cephalosporin-resistant and carbapenem-resistant Enterobacterales as critical pathogens.
Valmir Nascimento Rastely-Junior, Hosanea Santos Nascimento Rocha, Mitermayer Galvão Reis   +2 more
doaj   +2 more sources

Ambler class C-type β-lactamases and porin alterations in Enterobacter cloacae complex and Klebsiella aerogenes in the Netherlands, 2012–2023 [PDF]

BMC Microbiology
We investigated the genomic epidemiology of Ambler class C (AmpC-type) β-lactamases in Enterobacter cloacae complex and Klebsiella aerogenes in the national carbapenemase-producing Enterobacterales (CPE) surveillance of the Netherlands between 2012 and ...
Elke van Gorp, Simon Lansu, Cornelia C. H. Wielders, Angela de Haan, Gert-Jan Godeke, Sandra Witteveen, Jeroen Bos, Fabian Landman, Maureen Ouw, Herman F. Wunderink, Maurits P. A. van Meer, Wil van der Zwet, Daan W. Notermans, Antoni P. A. Hendrickx, A. L. E. van Arkel, M. A. Leversteijn-van Hall, W. van den Bijllaardt, R. van Mansfeld, K. van Dijk, B. Zwart, B. M. W. Diederen, H. Berkhout, A. Ott, K. Waar, W. Ang, J. da Silva, A. L. M. Vlek, J. J. J. M. Stohr, L. G. M. Bode, A. Jansz, S. Paltansing, A. J. van Griethuysen, J. R. Lo Ten Foe, M. J. C. A. van Trijp, M. Wong, A. E. Muller, M. P. M. van der Linden, M. van Rijn, S. B. Debast, E. Kolwijck, N. Al Naiemi, T. Schulin, S. Dinant, S. P. van Mens, D. C. Melles, J. W. T. Cohen Stuart, P. Gruteke, A. P. van Dam, I. Maat, B. Maraha, J. C. Sinnige, E. van der Vorm, M. P. A. van Meer, M. de Graaf, E. de Jong, S. J. Vainio, E. Heikens, M. den Reijer, J. W. Dorigo-Zetsma, A. Troelstra, E. Bathoorn, J. de Vries, D. W. van Dam, E. I. G. B. de Brauwer, R. Steingrover, F. Koene, C. Oliveira dos Santos   +66 more
doaj   +2 more sources

High in vitro activity of aztreonam/avibactam against NDM-producing Enterobacterales with emerging resistance in Escherichia coli in the United States Mid-Atlantic region [PDF]

Microbiology Spectrum
New Delhi metallo-β-lactamase (NDM)-producing Enterobacterales represent a critical antimicrobial resistance threat with limited therapeutic options. Aztreonam/avibactam, which combines the stability of aztreonam against metallo-β-lactamases with the ...
Eetu Eklund, Tyler Maruca, Kate Kruczynski, Heather Critchfield, Robert Murphy, Eric Keller, Benjamin Lee, Ami Patel, Liore Klein, David A. Torpey, Robert A. Myers, Victoria L. Campodónico   +11 more
doaj   +2 more sources

Prevalence of Extended Spectrum β-Lactamase, Metallo β-Lactamase, and AmpC β-Lactamase among Gram Negative Bacilli Recovered from Burn Wound Infection

RUHS Journal of Health Sciences, 2023
Introduction: Infections are the major cause of morbidity and mortality in burn patients. The ESBL, MBL and AmpC are the major mediators of antimicrobial resistance in gram negative bacteria. Early detection of ESBL, MBL and AmpC β -lactamases is crucial
Kusum Lata Lodha, Seema Surana
doaj   +1 more source

Molecular Characterization of AmpC β-lactamases in Enterobacteriaceae

Journal of Pure and Applied Microbiology, 2022
AmpC β-lactamases are enzymes that are resistant to β-lactams, such as penicillin and cephalosporin, but not cefoxitin and cefotetan. This study was conducted to characterize AmpC β-lactamases in Enterobacteriaceae.
D. Bindu, Chitralekha Saikumar
doaj   +1 more source

Plasmid Derived AmpC Genotypes among the Multidrug Resistant Enterobacteriaceae Strains Isolated from Urine Samples in Southern India [PDF]

Journal of Clinical and Diagnostic Research, 2021
Introduction: The most common pathogens causing Urinary Tract Infections (UTI) in community and hospital settings are Enterobacteriaceae. Antibiotic resistance is a major problem worldwide because of an increase in the use of antibiotics.
P Ronni Mol, Ganesan Shanthi, Khalid Bindayna   +2 more
doaj   +1 more source

An extended-spectrum AmpC-type β-lactamase obtained by in vitro antibiotic selection [PDF]

FEMS Microbiology Letters, 1998
A predictive approach was assayed to evaluate the possibility of mutant Amp-C beta-lactamase emergence with increased substrate spectrum (including new C-3' quaternary ammonium cephems). The ampC gene encoding the AmpC beta-lactamase from Enterobacter cloacae was cloned and expressed in an AmpC-defective strain of E. coli.
M I, Morosini, M C, Negri, B, Shoichet, M R, Baquero, F, Baquero, J, Blázquez   +5 more
openaire   +2 more sources