Results 11 to 20 of about 45,681 (215)

In vitro activity of cefiderocol against European Enterobacterales, including isolates resistant to meropenem and recentβ-lactam/β-lactamase inhibitor combinations

Microbiology Spectrum
Carbapenem-resistant Enterobacterales represent a major health threat and have few approved therapeutic options. Enterobacterales isolates were collected from hospitalized inpatients from 49 sites in six European countries (1 January–31 December 2020 ...
Anne Santerre Henriksen, Fabio Arena, Marie Attwood, Rafael Canton, Sören Gatermann, Thierry Naas, Ian Morrissey, Christopher Longshaw   +7 more
doaj   +3 more sources

Biochemical characterization of CTX-M-15 from Enterobacter cloacae and designing a novel non-β-lactam-β-lactamase inhibitor. [PDF]

PLoS ONE, 2013
The worldwide dissemination of CTX-M type β-lactamases is a threat to human health. Previously, we have reported the spread of bla(CTX-M-15) gene in different clinical strains of Enterobacteriaceae from the hospital settings of Aligarh in north India. In
Mohammad Faheem, Md Tabish Rehman, Mohd Danishuddin, Asad U Khan   +3 more
doaj   +2 more sources

Human metallo-β-lactamase enzymes degrade penicillin

Scientific Reports, 2019
Nonribosomal peptides are assemblages, including antibiotics, of canonical amino acids and other molecules. β-lactam antibiotics act on bacterial cell walls and can be cleaved by β-lactamases.
Seydina M. Diene, Lucile Pinault, Vivek Keshri, Nicholas Armstrong, Saber Khelaifia, Eric Chabrière, Gustavo Caetano-Anolles, Philippe Colson, Bernard La Scola, Jean-Marc Rolain, Pierre Pontarotti, Didier Raoult   +11 more
doaj   +2 more sources

Metallo-β-Lactamase Inhibitor Phosphonamidate Monoesters [PDF]

ACS Omega, 2022
Being the second leading cause of death and the leading cause of disability-adjusted life years worldwide, infectious diseases remaincontrary to earlier predictionsa major consideration for the public health of the 21st century. Resistance development of
Katarzyna Palica, Manuela Vorácová, Susann Skagseth, Anna Andersson Rasmussen, Lisa Allander, Madlen Hubert, Linus Sandegren, Hanna-Kirstirep Schrøder Leiros, Hanna Andersson, Máté Erdélyi   +9 more
doaj   +3 more sources

Comparative Evaluation of the in-vitro Activity of Six β-lactam/β-lactamase Inhibitor Combinations against Gram Negative Bacilli [PDF]

Journal of Clinical and Diagnostic Research, 2013
Background: The extensive use of the β-lactam antibiotics in hospitals and in the community has created major resistance problems which has led to increased morbidity, mortality and healthcare costs.
Smita Sood
doaj   +1 more source

Management of clinical infections of Escherichia coli by new β-lactam/ β-lactamase inhibitor combinations

Iranian Journal of Microbiology, 2022
Background and Objectives: Escherichia coli (E. coli) is an important member of Enterobacteriaceae family involved in severe infections. The increased rate of resistance towards different classes of antibiotics limits their treatment options. The aim of
Ashraf Ahmed Kadry, May Ayman El-Antrawy, Amira Mohammed El-Ganiny   +2 more
doaj   +1 more source

Characterization and amino acid sequence of IRT-4, a novel TEM-type enzyme with a decreased susceptibility to β-lactamase inhibitors [PDF]

FEMS Microbiology Letters, 1994
The clinical isolate Escherichia coli PEY was highly resistant to amoxycillin, ticarcillin and piperacillin associated to beta-lactamase inhibitors such as clavulanic acid, sulbactam, tazobactam and brobactam but susceptible to cephalosporins, aztreonam and imipenem.
T, Brun, J, Péduzzi, M M, Caniça, G, Paul, P, Névot, M, Barthélémy, R, Labia   +6 more
openaire   +2 more sources

Substitution of Met-69 by Ala or Gly in TEM-1 β-lactamase confer an increased susceptibility to clavulanic acid and other inhibitors [PDF]

FEMS Microbiology Letters, 2002
In some inhibitor-resistant TEM-derived beta-lactamases, Met-69 is substituted by Leu, Ile or Val. Residue 69 is located in a region of strong structural constraints, at the beginning of H2 alpha-helix, and in the vicinity of B3 and B4 beta-strands.
Stéphanie, Madec, Claudine, Blin, Rajagopal, Krishnamoorthy, Bertrand, Picard, El Bachir, Chaibi, Martine, Fouchereau-Péron, Roger, Labia   +6 more
openaire   +2 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

Substitution of Arg-244 by Cys or Ser in SHV-1 and SHV-5 β-lactamases confers resistance to mechanism-based inhibitors and reduces catalytic efficiency of the enzymes [PDF]

FEMS Microbiology Letters, 1998
The conserved residue Arg-244 was substituted by the smaller uncharged amino acids Cys and Ser in SHV-1 and SHV-5 beta-lactamases by a PCR-based site-specific mutagenesis procedure. The mutant beta-lactamases displayed decreased susceptibility to clavulanate and, to a lesser extent, to tazobactam and sulbactam.
Giakkoupi, P, Tzelepi, E, Legakis, NJ, Tzouvelekis, LS   +3 more
openaire   +3 more sources