Background: β-lactamase is an enzyme that plays a role in the occurrence of antibiotic resistance against Methicillin-resistant Staphylococcus aureus (MRSA) bacteria. Viscosin is a lipopeptide biosurfactant produced by the Pseudomonas group bacteria.
Mokhamad Fahmi Rizki Syaban +4 more
openaire +1 more source
Penetration of β-lactamase inhibitors into the periplasm of Gram-negative bacteria [PDF]
The effectiveness of a beta-lactamase inhibitor/beta-lactam combination against Gram-negative pathogens depends on many interplaying factors, one of which is the penetration of the inhibitor across the outer membrane. In this work we have measured the relative penetrations of clavulanic acid, sulbactam, tazobactam and BRL 42715 into two strains of ...
Farmer TH, Degnan BA, Payne DJ
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Outer membrane permeability of β-lactamase inhibitors inPseudomonas aeruginosa [PDF]
Evaluation of four beta-lactamase inhibitors in terms of their outer membrane permeability in Pseudomonas aeruginosa revealed that sulbactam and tazobactam diffused most efficiently and equally well. That of BRL42715 appeared to be a factor of ten lower than that of the above two, but it showed the strongest beta-lactamase inhibitory activity.
S, Satake, T, Nakae
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Characterization and amino acid sequence of IRT-4, a novel TEM-type enzyme with a decreased susceptibility to β-lactamase inhibitors [PDF]
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 +6 more
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Substitution of Met-69 by Ala or Gly in TEM-1 β-lactamase confer an increased susceptibility to clavulanic acid and other inhibitors [PDF]
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 +6 more
openaire +2 more sources
Novel IMP-1 metallo-β-lactamase inhibitors can reverse meropenem resistance inEscherichia coliexpressing IMP-1 [PDF]
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 +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]
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 +3 more
openaire +3 more sources
Abstract This narrative review summarizes the collective knowledge on periodontal microbiology, through a historical timeline that highlights the European contribution in the global field. The etiological concepts on periodontal disease culminate to the ecological plaque hypothesis and its dysbiosis‐centered interpretation.
Georgios N. Belibasakis +5 more
wiley +1 more source
Supra and subgingival application of antiseptics or antibiotics during periodontal therapy
Abstract Periodontal diseases (gingivitis and periodontitis) are characterized by inflammatory processes which arise as a result of disruption of the balance in the oral ecosystem. According to the current S3 level clinical practice guidelines, therapy of patients with periodontitis involves a stepwise approach that includes the control of the patient ...
Elena Figuero +5 more
wiley +1 more source
Repression of Virulence in Staphylococcus aureus by 2‐Aminothiol‐Mediated Quorum Quenching
Simple analogues of cysteine that can eliminate the native autoinducing peptides (AIPs) of staphylococci extracellularly, before they activate their receptor, and turn off quorum sensing in different Staphylococcus aureus. The elimination of AIPs occurs through a mechanism similar to native chemical ligation (NCL). Further, this strategy showed promise
Bengt H. Gless +5 more
wiley +2 more sources

