Study of β-Lactam antibiotic susceptibilites and characteristics of penicillin-binding proteins from Streptococcus anginosus, S. constellatus and S. intermedius

1996 ◽  
Vol 2 (4) ◽  
pp. 222-231
Author(s):  
Hiroyuki Usui
Keyword(s):  
Binding Proteins ◽  
Penicillin Binding Proteins ◽  
Streptococcus Anginosus ◽  
Lactam Antibiotic

β-Lactam antibiotic targets and resistance mechanisms: from covalent inhibitors to substrates

2021 ◽  
Author(s):  
Montserrat Mora-Ochomogo ◽  
Christopher T. Lohans
Keyword(s):  
Binding Proteins ◽  
Resistance Mechanisms ◽  
Penicillin Binding Proteins ◽  
Covalent Inhibitors ◽  
Lactam Antibiotic

Overview of β-lactam antibiotics and the proteins with which they covalently interact, focusing on penicillin-binding proteins and serine β-lactamases.

Binding of a non-β-lactam antibiotic to penicillin-binding proteins

Nature ◽  
1987 ◽  
Vol 325 (6100) ◽  
pp. 179-180 ◽  
Author(s):  
Y. Nozaki ◽  
N. Katayama ◽  
H. Ono ◽  
S. Tsubotani ◽  
S. Harada ◽  
...  
Keyword(s):  
Binding Proteins ◽  
Penicillin Binding Proteins ◽  
Lactam Antibiotic

scholarly journals Kinetics of penicillin binding to penicillin-binding proteins of Staphylococcus aureus

1994 ◽  
Vol 301 (1) ◽  
pp. 139-144 ◽  
Author(s):  
H F Chambers ◽  
M J Sachdeva ◽  
C J Hackbarth
Keyword(s):  
Staphylococcus Aureus ◽  
Binding Proteins ◽  
Beta Lactam ◽  
Penicillin Binding Proteins ◽  
Structural Modifications ◽  
Drug Concentrations ◽  
Lactam Antibiotic ◽  
Resistant Strains ◽  
The Relationship ◽  
Kinetics Of

Reduced affinity of penicillin-binding proteins (PBPs) for binding penicillin has been proposed as a mechanism of beta-lactam antibiotic resistance in staphylococci. Penicillin binding by PBPs of three penicillin-susceptible and two penicillin-resistant strains of Staphylococcus aureus was studied in kinetic assays to determine rate constants, drug concentrations at which PBPs were bound and the relationship between concentrations that bound PBPs and concentrations that inhibited bacterial growth. PBPs 1 and 2 of the resistant strains exhibited slower acylation and more rapid deacylation than susceptible strains. In contrast PBP 4, a naturally low-affinity PBP, was modified such that it exhibited a lower rate of deacylation. The concentrations of penicillin at which modified PBPs were bound correlated with concentrations that inhibited growth of the resistant strains. Acquisition of penicillin resistance in these strains of S. aureus results, at least in part, from structural modifications affecting binding of multiple PBPs and appears to include recruitment of a non-essential PBP, PBP 4.

Effect of piperacillin on morphology and viability of gram-negative bacteria

1984 ◽  
Vol 42 ◽  
pp. 218-219
Author(s):  
R. H. Liss
Keyword(s):  
Inhibitory Concentration ◽  
Cytoplasmic Membrane ◽  
Drug Binding ◽  
Gram Negative Bacteria ◽  
Bacterial Cells ◽  
Drug Induced ◽  
Penicillin Binding Proteins ◽  
Lactam Antibiotic ◽  
Drug Free ◽  
Tube Dilution

Piperacillip (PIP) is b-[D(-)-α-(4-ethy1-2,3-dioxo-l-piperzinylcar-bonylamino)-α-phenylacetamido]-penicillanate. The broad spectrum semisynthetic β-lactam antibiotic is believed to effect bactericidal activity through its affinity for penicillin-binding proteins (PBPs), enzymes on the bacterial cytoplasmic membrane that control elongation and septation during cell growth and division. The purpose of this study was to correlate penetration and binding of 14C-PIP in bacterial cells with drug-induced lethal changes assessed by microscopic, microbiologic and biochemical methods.The bacteria used were clinical isolates of Escherichia coli and Pseudomonas aeruginosa (Figure 1). Sensitivity to the drug was determined by serial tube dilution in Trypticase Soy Broth (BBL) at an inoculum of 104 organisms/ml; the minimum inhibitory concentration of piperacillin for both bacteria was 1 μg/ml. To assess drug binding to PBPs, the bacteria were incubated with 14C-PIP (5 μg/0.09 μCi/ml); controls, in drug-free medium.

scholarly journals Enterobactin- and salmochelin-β-lactam conjugates induce cell morphologies consistent with inhibition of penicillin-binding proteins in uropathogenic Escherichia coli CFT073

2021 ◽  
Author(s):  
Artur Sargun ◽  
Timothy C. Johnstone ◽  
Hui Zhi ◽  
Manuela Raffatellu ◽  
Elizabeth M. Nolan
Keyword(s):  
Escherichia Coli ◽  
Binding Proteins ◽  
Uropathogenic Escherichia Coli ◽  
Penicillin Binding Proteins ◽  
E Coli

Siderophore-β-lactam conjugates based on enterobactin and diglucosylated enterobactin enter the periplasm of uropathogenic E. coli CFT073 via the FepA and IroN transporters, and target penicillin-binding proteins.

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