Results 121 to 130 of about 58,396 (229)

Clinical Epidemiological Analysis of the Genotypic Spectrum and Mortality Risk in Carbapenem‐Resistant Klebsiella pneumoniae (CRKP) Infections

Canadian Journal of Infectious Diseases and Medical Microbiology, Volume 2026, Issue 1, 2026.
Background Carbapenem‐resistant Klebsiella pneumoniae (CRKP) has become a global public health threat, with significantly increased morbidity and mortality among high‐risk inpatients. High‐risk genotypes of CRKP, primarily including K. pneumoniae carbapenemase (KPC), oxacillinase‐48–like (OXA‐48–like), New Delhi metallo‐β‐lactamase (NDM), imipenemase ...
Qiongfang Zhang, Ze Fang, Bo Fang, Hailing Zeng, Jiaojiao Xu, Muhammad Abu Bakr Shabbir   +5 more
wiley   +1 more source

Evidence for a Dinuclear Active Site in the Metallo-β-lactamase BcII with Substoichiometric Co(II): A New Model for Uptake [PDF]

, 2007
Metallo-β-lactamases are zinc-dependent enzymes that constitute one of the main resistance mechanisms to β-lactam antibiotics. Metallo-β-lactamases have been characterized both in mono- and dimetallic forms.
Bennett, Brian, Kowalski, Jason M., Llarrull, Leticia l., Tioni, Mariana F., Vila, Alejandro J.   +4 more
core   +1 more source

Insights of β‐Lactams Resistance in Klebsiella pneumoniae Clinical Isolates: A Focus on Molecular Identification of Drug Resistance

International Journal of Microbiology, Volume 2026, Issue 1, 2026.
Klebsiella pneumoniae is associated with high antimicrobial resistance and is commonly isolated from colonization and healthcare‐associated infections (HAIs). This study is aimed at developing and validating molecular assays to detect resistance genes belonging to the bla family in resistant K. pneumoniae isolates.
Lavouisier F. B. Nogueira, Marília S. Maia, Marco A. F. Clementino, Ila F. N. Lima, Jorge L. N. Rodrigues, Luciana V. C. Fragoso, Glairta S. Costa, Jose Q. S. Filho, Alexandre Havt, Deiziane V. S. Costa, Lyvia M. V. C. Magalhães, Dilza Silva, José K. Sousa, Aldo A. M. Lima, Divakar Sharma   +14 more
wiley   +1 more source

Asp-120 Locates Zn2 for Optimal Metallo-β-lactamase Activity [PDF]

, 2007
Metallo-β-lactamases are zinc-dependent hydrolases that inactivate β-lactam antibiotics, rendering bacteria resistant to them. Asp-120 is fully conserved in all metallo-β-lactamases and is central to catalysis.
Bennett, Brian, Fabiane, Stella M., Kowalski, Jason M., Llarrull, Leticia l., Sutton, Brian J., Vila, Alejandro J.   +5 more
core   +1 more source

Reappraisal of hospital-acquired pneumonia mortality in the era of metallo-β-lactamase-mediated multidrug resistance: a prospective observational study [PDF]

, 2006
Introduction Hospital-acquired pneumonia (HAP) due to Pseudomonas aeruginosa is associated with high mortality rates. The metallo-β-lactamases (MBLs) are emerging enzymes that hydrolyze virtually all β-lactams. We aimed to assess P.
Zavascki, Alexandre Prehn, Barth, Afonso Luis, Fernandes, Juliana Fernandez, Moro, Ana Lúcia Didonet, Gonçalves, Ana Lúcia Saraiva, Goldani, Luciano Zubaran   +5 more
core   +1 more source

Metallo-β-lactamase and genetic diversity of Pseudomonas aeruginosa in intensive care units in Campo Grande, MS, Brazil

Brazilian Journal of Infectious Diseases
Infection by Pseudomonas aeruginosa has spread worldwide, with limited options for treatment. The purpose of this study was to investigate metallo-β-lactamase-producing P.
Ana Claudia Souza Rodrigues, Marilene Rodrigues Chang, Gabriela Dorn Nóbrega, Mayara Souza Rodrigues, Nadia Cristina Pereira Carvalho, Beatriz Garcia Gomes, Dênio Lopes de Almeida, Karyne Rangel Carvalho, Marise Dutra Asensi   +8 more
doaj   +1 more source

Evolution of New Delhi metallo-β-lactamase (NDM) in the clinic: Effects of NDM mutations on stability, zinc affinity, and mono-zinc activity

Journal of Biological Chemistry, 2018
Infections by carbapenem-resistant Enterobacteriaceae are difficult to manage owing to broad antibiotic resistance profiles and because of the inability of clinically used β-lactamase inhibitors to counter the activity of metallo-β-lactamases often ...
Zishuo Cheng, P. Thomas, Lincheng Ju, Alexander Bergstrom, K. Mason, Delaney Clayton, Callie Miller, C. Bethel, J. Vanpelt, D. Tierney, R. Page, R. Bonomo, W. Fast, M. Crowder   +13 more
semanticscholar   +1 more source

In House Rapid, Simple Multiple‐Locus Variable‐Number Tandem Repeat Analysis (MLVA): A Reliable Tool for Enterobacter hormaechei Genotyping

MicrobiologyOpen, Volume 14, Issue 6, December 2025.
We developed a new MLVA protocol targeting eight VNTR loci for the rapid and cost‐effective surveillance of Enterobacter hormaechei. Tested on diverse clinical isolates, it showed a discriminatory power comparable to MLST and was able to distinguish some strains within the same sequence type.
Claire Guillermard, Audrey Baron, Philippe Bidet, Kevin La, Maud Gits‐Muselli, Céline Courroux, Célie Malaure, Laurent Dortet, André Birgy, Stéphane Bonacorsi   +9 more
wiley   +1 more source

Molecular characterization of blaNDM-5 carried in an IncFII plasmid in Escherichia coli from a non-traveller patient in Spain. [PDF]

, 2016
A carbapenem-resistant Escherichia coli isolate (sequence type 448 [ST448]) was recovered from a urine culture of a female patient with no recent record of traveling.
Marco Reverté, Francesc, Moreno Camacho, Ma. Asunción, Pitart, Cristina, Roca Subirà, Ignasi, Román, Angely, Solé, Mar, Vila Estapé, Jordi   +6 more
core   +1 more source

Prevalence of metallo-β-lactamase-encoding genes among carbapenem-resistant Pseudomonas aeruginosa strains isolated from burn patients in Iran

Revista da Sociedade Brasileira de Medicina Tropical
Carbapenem-resistant Pseudomonas aeruginosa (CRPA) has been considered a major cause of infection and mortality in burn patients, especially in developing countries such as Iran. One of the most common mechanisms of carbapenem resistance is production of
Fereshteh Jabalameli, Elahe Taki, Mohammad Emaneini, Reza Beigverdi   +3 more
doaj   +1 more source