Virulence of non-β-lactamase-mediated ampicilin-resistantHaemophilus influenzae [PDF]
We questioned whether strains of ampicillin-resistant, non-β-lactamase-producing (AmpR NBLP) Haemophilus influenae with lower affinity penicillin-binding proteins (PBPs) might have altered virulence. The virulence of resistant transformant strains and the susceptible recipient was compared using infant rats. Following intraperitoneal inoculation, there
Lorry G. Rubin +3 more
openaire +1 more source
Distribution of β-lactamase genes of Klebsiella pneumoniae isolates in Zhejiang province, China, and regulation of gene expression [PDF]
Klebsiella pneumoniae is a common causative agent of nosocomial infections with a high level of resistance toward β-lactam antibiotics. Our previous study showed that TEM-1 and SHV-11 are the predominant β-lactamase-encoding genes of K ...
Zhao Jin-Fang +5 more
doaj +1 more source
LXA-1: a new plasmid-mediated β-lactamase giving low-level resistance [PDF]
LXA-1, a novel plasmid-mediated β-lactamase, was observed in clinical isolates of Klebsiella oxytoca, Klebsiella pneumoniae, Citrobacter freundii and Enterobacter cloacae. All the strains additionally produced TEM-1 β-lactamase. LXA-1 had an Mr of 24 000 and a pI of 6.7.
Youjun Yang, G.A. Jacoby, D.M. Livermore
openaire +1 more source
Fluorescent Mesoporous Nanoparticles for β‐Lactamase Screening Assays
We present a sensitive and rapid screening method for the determination of β‐lactamase activity of antibiotic‐resistant bacteria, by designing a pH‐sensitive fluorescent dye‐doped mesoporous silica nanoparticle encapsulated with penicillin G as a ...
Srikrishna Tummala +4 more
doaj +1 more source
Various Extracts of Some Medicinal Plants as Inhibitors for Beta-lactamase Activity
The inhibitory effect of acetone, ethanol, and aqueous extracts of ten medicinal plants on β-lactamase from Staphylococcus sciuri and Klebsiella pneumoniae was investigated in vitro by starch-iodine agar plate method.
Huda S. A. Al-Hayanni, Hamed El-Shora
doaj +1 more source
The Mechanisms of Catalysis by Metallo β-Lactamases [PDF]
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 +3 more
core +3 more sources
Prevalence of 16S rRNA methylase genes among β-lactamase-producing Enterobacteriaceae clinical isolates in Saudi Arabia [PDF]
Background: Co production of 16S rRNA methylases gene and β-Lactamase gene among Enterobacteriaceae isolates conferring resistance to both therapeutic options has serious implications for clinicians worldwide.
Yazeed A. Al Sheikh +4 more
doaj +1 more source
High colonization rates of extended-spectrum β-lactamase (ESBL)-producing Escherichia coli [PDF]
BACKGROUND International travel contributes to the worldwide spread of multidrug resistant Gram-negative bacteria. Rates of travel-related faecal colonization with extended-spectrum β-lactamase (ESBL)-producing Enterobacteriaceae vary for different ...
Battegay, Manuel +25 more
core +3 more sources
Isolation and preliminary characterization of β-lactamase excretory mutants ofEscherichia coliK-12 [PDF]
Abstract Escherichia coli exc mutants able to release the plasmid pBR322-encoded β-lactamase (EC 3.5.2.6) into the extracellular medium have been isolated using a new in situ plate assay. A preliminary characterization of the exc mutants was carried out: the presence of exc mutations was associated with a specific or pleiotropic pattern of ...
Nicole Fognini-Lefebvre +1 more
openaire +1 more source
Broad antibiotic resistance profile of the subclass B3 metallo-β-lactamase GOB-1, a di-zinc enzyme. [PDF]
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 +26 more
core +1 more source

