Results 11 to 20 of about 86,850 (260)

RelQ Mediates the Expression of β-Lactam Resistance in Methicillin-Resistant Staphylococcus aureus [PDF]

open access: yesFrontiers in Microbiology, 2019
An induced stringent response, which is established by an increased level of (p)ppGpp, is required for the expression of β-lactam resistance in methicillin-resistant Staphylococcus aureus (MRSA).
Ajita Bhawini   +6 more
doaj   +2 more sources

Important role of a putative lytic transglycosylase Cj0843c in β-lactam resistance in Campylobacter jejuni

open access: yesFrontiers in Microbiology, 2015
Beta-lactam antibiotics are an important class of antibiotics for treating bacterial infections. Despite prevalent β-lactam resistance in Campylobacter jejuni, the leading bacterial cause of human diarrhea in developed countries, molecular mechanism of β-
Ximin eZeng   +2 more
doaj   +2 more sources

Molecular basis of β-lactam antibiotic resistance of ESKAPE bacterium E. faecium Penicillin Binding Protein PBP5

open access: yesNature Communications, 2023
Penicillin-binding proteins (PBPs) are essential for the formation of the bacterial cell wall. They are also the targets of β-lactam antibiotics. In Enterococcus faecium, high levels of resistance to β-lactams are associated with the expression of PBP5 ...
Yamanappa Hunashal   +10 more
doaj   +2 more sources

β-Lactam Antibiotics Renaissance

open access: yesAntibiotics, 2014
Since the 1940s β-lactam antibiotics have been used to treat bacterial infections. However, emergence and dissemination of β-lactam resistance has reached the point where many marketed β-lactams no longer are clinically effective.
Wenling Qin   +2 more
doaj   +2 more sources

Thefiblocus inStreptococcus pneumoniaeis required for peptidoglycan crosslinking and PBP-mediated β-lactam resistance [PDF]

open access: yesFEMS Microbiology Letters, 2000
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
openaire   +2 more sources

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

Restoration of effectiveness of β-lactams on methicillin-resistantStaphylococcus aureusby tellimagrandin I from rose red [PDF]

open access: yesFEMS Microbiology Letters, 2000
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
openaire   +2 more sources

Loss of GdpP Function in Staphylococcus aureus Leads to β-Lactam Tolerance and Enhanced Evolution of β-Lactam Resistance [PDF]

open access: yes, 2022
Infections caused by Staphylococcus aureus are a leading cause of mortality. Treating infections caused by S. aureus is difficult due to resistance against most traditional antibiotics, including β-lactams.
Huang, Liusheng   +15 more
core   +1 more source

Resistance to β-lactam antibiotics conferred by point mutations in penicillin-binding proteins PBP3, PBP4 and PBP6 in Salmonella enterica. [PDF]

open access: yesPLoS ONE, 2014
Penicillin-binding proteins (PBPs) are enzymes responsible for the polymerization of the glycan strand and the cross-linking between glycan chains as well as the target proteins for β-lactam antibiotics.
Song Sun, Maria Selmer, Dan I Andersson
doaj   +1 more source

Substitution of Thr for Ala-237 in TEM-17, TEM-12 and TEM-26: alterations in β-lactam resistance conferred onEscherichia coli [PDF]

open access: yesFEMS Microbiology Letters, 2001
Non-naturally occurring mutants of TEM-17 (E104K), TEM-12 (R164S) and TEM-26 (E104K:R164S) extended-spectrum (ES) beta-lactamases bearing threonine at position 237 were constructed by site-specific mutagenesis and expressed under isogenic conditions in Escherichia coli.
Giakkoupi, P.   +5 more
openaire   +4 more sources

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