Results 21 to 30 of about 893,574 (181)

Identification and characterization of a novel metallo β-lactamase, SZM-1, in Shenzhen Bay, South China

Frontiers in Microbiology, 2022
Metallo β-Lactamases (MBLs) degrade most clinical β-lactam antibiotics, especially Carbapenem, posing a huge threat to global health. Studies on environmental MBLs are important for risk assessment of the MBLs transmission among connected habitats, and ...
Lingxu Fang, Zongbao Liu, Zhongyi Lu, Zhongyi Lu, Rongzhong Huang, Rong Xiang   +5 more
doaj   +1 more source

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

Cefiderocol: An Overview of Its in-vitro and in-vivo Activity and Underlying Resistant Mechanisms

Frontiers in Medicine, 2021
Treatment of multidrug-resistant (MDR) Gram-negative bacteria (GNB) infections has led to a global public health challenging due to the bacterial resistance and limited choices of antibiotics.
Jiahui Yao, Jin Wang, Mengli Chen, Yun Cai   +3 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

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

Metallo-β-lactamases producing Gram negative isolates from VAP patients.

, 2021
Metallo-β-lactamases producing Gram negative isolates from VAP patients.
Suhail Sarwar Siddiqui (11408618), Prashant Gupta (4046920), Piyush Tripathi (5567492), Ved Prakash (4970143), Mithlesh Kumari (11408615), Sheetal Verma (5225192), Avinash Agarwal (6823241), Vimala Venkatesh (41044), Zia Arshad (4969093)   +8 more
core   +1 more source

Identification of 76 novel B1 metallo-β-lactamases through large-scale screening of genomic and metagenomic data

Microbiome, 2017
Background Metallo-β-lactamases are bacterial enzymes that provide resistance to carbapenems, the most potent class of antibiotics. These enzymes are commonly encoded on mobile genetic elements, which, together with their broad substrate spectrum and ...
Fanny Berglund, Nachiket P. Marathe, Tobias Österlund, Johan Bengtsson-Palme, Stathis Kotsakis, Carl-Fredrik Flach, D G Joakim Larsson, Erik Kristiansson   +7 more
doaj   +1 more source

Time-resolved β-lactam cleavage by L1 metallo-β-lactamase

Nature Communications, 2022
Metallo-β-lactamases cleave β-lactam moiety of many broadly used antibiotics. Here the authors captured mechanistic details of the enzyme catalyzed reaction using time-resolved xray synchrotron serial crystallography.
M. Wilamowski, D. A. Sherrell, Y. Kim, A. Lavens, R. W. Henning, K. Lazarski, A. Shigemoto, M. Endres, N. Maltseva, G. Babnigg, S. C. Burdette, V. Srajer, A. Joachimiak   +12 more
doaj   +1 more source