BACKGROUND Penicillin-binding proteins (PBPs) are well known and validated targets for antibacterial therapy. The most important clinically used inhibitors of PBPs β-lactams inhibit transpeptidase activity of PBPs by forming a covalent penicilloyl-enzyme complex that blocks the normal transpeptidation reaction; this finally results in bacterial death. In some resistant bacteria the resistance i...

The penicillin-binding proteins (PBPs) of a methicillin-resistant (MR) and a methicillin-susceptible (MS) Staphylococcus aureus were compared by various approaches involving the use of high-specific-activity [3H]penicillin as a reagent. The MR and MS strains were found to contain PBPs of the same number and electrophoretic mobilities. However, saturation of PBPs 1, 2, and 3 by methicillin in th...

Abstract Streptococcus pneumoniae is one of the most frequent bacterial identified causes community-acquired pneumonia, otitis media and meningitis. It is, as well, a common cause bacteraemia’s significant morbidity mortality. Beta-lactam antibiotics (BLAs) are first line empirical treatment for pneumococcal infections. The targets BLAs penicillin-binding proteins (PBPs), modifications which re...

Recently, interface management has been regarded as the key to success of prefabricated building projects (PBPs) due its capabilities manage numerous interfaces caused by PBPs’ inherent geographical and organizational fragmentation. However, factors influencing PBPs are largely unknown poorly studied. To compensate for this gap, study aimed investigate critical in with quantitative qualitative ...

Avibactam is a novel non-β-lactam β-lactamase inhibitor that covalently acylates a variety of β-lactamases, causing inhibition. Although avibactam presents limited antibacterial activity, its acylation ability toward bacterial penicillin-binding proteins (PBPs) was investigated. Staphylococcus aureus was of particular interest due to the reported β-lactamase activity of PBP4. The binding of avi...

Actinobacillus pleuropneumoniae, which was formerly classified in the genus Haemophilus, is a pathogen causing swine pleuropneumonia. We found that aspoxicillin showed strong activity and that meropenem had better lytic activity against this pathogen. In the present study, we for the first time identified penicillin-binding proteins (PBPs) of A. pleuropneumoniae in order to elucidate the relati...

The penicillin-binding proteins (PBPs) of four species of the genus Bacteroides were examined in cell envelope preparations from exponentially growing cultures and intact cells. Upon examination by sodium dodecyl sulfate-polyacrylamide electrophoresis, three major high-molecular-weight PBPs (molecular weight, 58,000 to 82,000) were resolved, and low-molecular-weight PBPs were seen in all strain...

The penicillin-binding proteins (PBPs) are a set of enzymes that participate in bacterial peptidoglycan assembly. The absolute numbers of each PBP were determined by direct measurement and have been reported for two Staphylococcus aureus strains, RN4220 (methicillin-sensitive S. aureus) and RN450M (methicillin-resistant S. aureus). From the specific activity of the labeled penicillin and the ab...

A simple assay for detection of compounds that bind to the active site in the transglycosylation domain of the essential bifunctional transglycosylase and transpeptidase penicillin-binding proteins (PBPs) is reported. The method is based on a competition with the specific transglycosylase inhibitor moenomycin. With moenomycin coupled to Affi-Gel beads, a simple filtration procedure allows the a...

Penicillin-binding proteins (PBPs) are responsible for peptidoglycan synthesis. By using biotinylated ampicillin, we detected PBPs of Lactobacillus paracasei strains. Ten PBPs were identified, 7 of which had apparent molecular sizes similar to those of Escherichia coli. In the presence of cholate, strain NRIC 0625 showed an elongated shape, and its putative PBP3 showed cholate-sensitive penicil...