Results 21 to 30 of about 54,273 (155)

Salicylate decreases production of AmpC type β-lactamases and increases susceptibility to β-lactams in aMorganella morganiiclinical isolate [PDF]

open access: yesFEMS Microbiology Letters, 2004
The effect of salicylate, a marRAB inducer, on the resistance to β-lactams was characterized in an AmpC β-lactamase hyperproducer Morganella morganii clinical isolate (the M1 strain). Results were compared with those of the effect of salicylate in a wild-type M. morganii strain.
María M. Tavío   +6 more
openaire   +1 more source

Transcending the challenge of evolving resistance mechanisms in Pseudomonas aeruginosa through β-lactam-enhancer-mechanism-based cefepime/zidebactam

open access: yesmBio, 2023
Multi-drug resistant (MDR) Pseudomonas aeruginosa harbor a complex array of β-lactamases and non-enzymatic resistance mechanisms. In this study, the activity of a β-lactam/β-lactam-enhancer, cefepime/zidebactam, and novel β-lactam/β-lactamase inhibitor ...
Andrea M. Hujer   +14 more
doaj   +1 more source

β-Lactam induction of colanic acid gene expression inEscherichia coli [PDF]

open access: yesFEMS Microbiology Letters, 2003
An unexpected observation led us to examine the relationship between beta-lactam exposure and synthesis of colonic acid capsular polysaccharide in Escherichia coli. Strains containing a cps-lacZ transcriptional fusion were challenged with antibiotics having various modes of action, and gene expression was detected by a disk-diffusion assay and in broth
Frances C, Sailer   +2 more
openaire   +2 more sources

Effect of β-Lactamase inhibitors on in vitro activity of β-Lactam antibiotics against Burkholderia cepacia complex species

open access: yesAntimicrobial Resistance and Infection Control, 2016
Background Bacteria belonging to the Burkholderia cepacia complex (Bcc) are an important cause of chronic respiratory tract infections in cystic fibrosis patients.
Annelien Everaert, Tom Coenye
doaj   +1 more source

Synergistic Combinations of FDA-Approved Drugs with Ceftobiprole against Methicillin-Resistant Staphylococcus aureus

open access: yesMicrobiology Spectrum, 2023
New strategies are urgently needed to address the public health threat of antimicrobial resistance. Synergistic agent combinations provide one possible pathway toward addressing this need and are also of fundamental mechanistic interest.
Amar Deep Sharma, William G. Gutheil
doaj   +1 more source

Involvement of O8-antigen in altering β-lactam antibiotic susceptibilities inEscherichia coli [PDF]

open access: yesFEMS Microbiology Letters, 2008
In spite of being dispensable, O-antigens are believed to facilitate various cellular processes and alter antibiotic sensitivities. Escherichia coli K-12 (CS109) strains are lacking in O-antigens and are reported to be sensitive to antibiotics. To our surprise, E. coli 2443 (expressing O8-antigen) manifested two- to fourfold higher sensitivities toward
Sujoy K, Sarkar, Anindya S, Ghosh
openaire   +2 more sources

FtsH Sensitizes Methicillin-Resistant Staphylococcus aureus to β-Lactam Antibiotics by Degrading YpfP, a Lipoteichoic Acid Synthesis Enzyme

open access: yesAntibiotics, 2021
In the Gram-positive pathogen Staphylococcus aureus, FtsH, a membrane-bound metalloprotease, plays a critical role in bacterial virulence and stress resistance.
Won-Sik Yeo   +6 more
doaj   +1 more source

Detection of an IS21 insertion sequence in the mexR gene of Pseudomonas aeruginosa increasing β-lactam resistance [PDF]

open access: yesFEMS Microbiology Letters, 2004
To understand the regulation of the MexAB OprM efflux system in a clinical strain of Pseudomonas aeruginosa presenting a decreased susceptibility to ticarcillin and aztreonam, the mexR repressor gene was amplified by polymerase chain reaction (PCR) and was shown to be disrupted by an insertion sequence of more than 2 kb, with characteristic direct and ...
Boutoille, David   +7 more
openaire   +2 more sources

Reversible inactivation of a peptidoglycan transpeptidase by a β-lactam antibiotic mediated by β-lactam-ring recyclization in the enzyme active site

open access: yesScientific Reports, 2017
β-lactam antibiotics act as suicide substrates of transpeptidases responsible for the last cross-linking step of peptidoglycan synthesis in the bacterial cell wall.
Zainab Edoo   +2 more
doaj   +1 more source

Characterization of the membrane sensor PenJ for β-lactam antibodies fromBacillus licheniformisby amino acid substitution [PDF]

open access: yesFEMS Microbiology Letters, 1993
The PenJ protein of the penicillinase gene (penP) expression system from Bacillus licheniformis is an antirepressor and membrane receptor for beta-lactam antibiotics. A putative beta-lactam antibiotic binding site including Ser402 and Lys405, which are homologous to the conserved sequence for the beta-lactam binding site (Ser-X-X-Lys) is present.
M, Takagi, T, Ohta, S, Johki, T, Imanaka
openaire   +2 more sources

Home - About - Disclaimer - Privacy