K. pneumoniae resistance to β-lactam antibiotics is a public health problem. The objective was to characterize by molecular epidemiology isolates of K.
Lisbeth Carolina Sierra +3 more
doaj +1 more source
Most isolated strains of Staphylococcus sciuri contain mecA1, the evolutionary origin of mecA, but are sensitive to β-lactams (OS-MRSS, oxacillin-susceptible mecA1-positive S. sciuri).
Yifei Cai +12 more
doaj +1 more source
Detection of an IS21 insertion sequence in the mexR gene of Pseudomonas aeruginosa increasing β-lactam resistance [PDF]
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
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Thefiblocus inStreptococcus pneumoniaeis required for peptidoglycan crosslinking and PBP-mediated β-lactam resistance [PDF]
Penicillin resistance in pneumococci is mediated by modified penicillin-binding proteins (PBPs) that have decreased affinity to beta-lactams. In high-level penicillin-resistant transformants of the laboratory strain Streptococcus pneumoniae R6 containing various combinations of low-affinity PBPs, disruption of the fib locus results in a collapse of PBP-
B, Weber +5 more
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An update on the synthesis and reactivity of spiro-fused β-lactams
Beta-Lactam ring-containing compounds play a pivotal role in drug design and synthetic chemistry. Spirocyclic beta-lactams, representing an important beta-lactam subclass, have recently attracted considerable interest with respect to new synthetic methodologies and pharmacological applications.
Dao Thi, Hang, D'hooghe, Matthias
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Characterization of the membrane sensor PenJ for β-lactam antibodies fromBacillus licheniformisby amino acid substitution [PDF]
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
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Synthesis of Some New Mono- and Bis-Polycyclic Aromatic Spiro and Bis-Nonspiro-β-Lactams
Some new mono-and bis-polycyclic aromatic spiro-β-lactams and bis-non spiro-polycyclic aromatic β-lactams have been synthesized from imines derived from anthracene-9-carbaldehyde, 2-naphtaldehyde and a ketene derived from 9H-xanthene-9-carboxylic acid ...
Edris Ebrahimi, Aliasghar Jarrahpour
doaj +1 more source
High serum β-lactams specific/total IgE ratio is associated with immediate reactions to β-lactams antibiotics. [PDF]
Total serum IgE result from the combination of specific and non-specific pools. High specific/total IgE ratio may reflect high level of allergen-specific IgE on mast cells. No data regarding its applications to drug allergies is available.
Alessandra Vultaggio +5 more
doaj +1 more source
Restoration of effectiveness of β-lactams on methicillin-resistantStaphylococcus aureusby tellimagrandin I from rose red [PDF]
We found that extract from petals of Rosa canina L. (rose red) strikingly reduced the minimum inhibitory concentration of beta-lactams in methicillin-resistant Staphylococcus aureus. We isolated two compounds that reduced the minimum inhibitory concentrations of beta-lactams from the extract, tellimagrandin I and rugosin B.
S, Shiota +6 more
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Decreased membrane permeability in a polymyxin B-resistantEscherichia colimutant exhibiting multiple resistance to β-lactams as well as aminoglycosides [PDF]
A laboratory mutant of Escherichia coli stably resistant to more than 36,000 U ml-1 of polymyxin B was isolated. The mutant exhibited moderate increases in minimum inhibitory concentration to fluoroquinolones and bacitracin but high levels of cross-resistance to beta-lactams and aminoglycosides.
S O, Rahaman +3 more
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