Escherichia coli cells lacking low molecular weight penicillin binding proteins (LMW PBPs) exhibit morphological alterations that also appear when the septal protein FtsZ is mislocalized, suggesting that peptidoglycan modification and division may work together to produce cell shape. We found that in strains lacking PBP5 and other LMW PBPs, higher FtsZ concentrations increased the frequency of ...

The amino acid compositions of the radioactive peptides obtained from trypsin digestion of [14C]benzylpenicillin-labeled penicillin-binding proteins (PBPs) 1A, 1B, and 3 of Escherichia coli have been obtained. Complete digestion of these peptides with a combination of aminopeptidase M and carboxypeptidase Y showed that benzylpenicillin was bound to a serine residue in each of these proteins. Co...

Cyanobacteria are considered to be a potential source of novel bioactive compounds that are highly intriguing from biotechnological perspective. A number of bioactive compounds such as cyanotoxins, mycosporine-like amino acids (MAAs), scytonemin, phycobiliproteins (PBPs), phytohormones etc. have been reported from diverse group of cyanobacteria that show assorted biological activities ranging f...

A series of step-level penicillin-resistant derivatives of Streptococcus sanguis V288 (Challis) were obtained through successive genetic transformations. The DNA donor used was a laboratoryderived, penicillin-resistant multistep mutant of the recipient strain. Detection of the penicillinbinding proteins (PBPs) of wild-type and transformants revealed five major PBPs. While it was found that S. s...

OBJECTIVES The Vermont Oxford Network is a group of health professionals who are committed to improving the quality and safety of medical care for newborn infants and their families. Neonatal Intensive Care Quality Improvement Collaborative Year 2000 (NIC/Q 2000) was the second in a series of multiorganization improvement collaboratives organized and administered by the Vermont Oxford Network. ...

The nucleotide sequence of a 3,378-bp DNA fragment of Streptococcus pneumoniae that included the structural gene for penicillin-binding protein (PBP) 1a (ponA), which encodes 719 amino acids, was determined. Homologous DNA fragments from an S. oralis strain were amplified with ponA-specific oligonucleotides. The 2,524-bp S. oralis sequence contained the coding region for the first 636 amino aci...

This review covers the uses of fluorescence polarization and anisotropy for the investigation of bacterial penicillin binding proteins (PBPs), which are the targets of β-lactam antibacterial drugs (penicillins, cephalosporins, carbapenems, and monobactams), and of the β-lactamase enzymes that destroy these drugs and help to render bacterial pathogens resistant to them. Fluorescence polarization...

An approach of using molinspiration calculations and molecular docking on PBPs (penicillin-binding proteins) and certain β-lactamases is employed to predict the molecular properties, bioactivity and resistance of newer and reference cephalosporins. The previously synthesized cephalosporins 1-8 and reference cephalosporins were subjected to extensive evaluations by calculating the molecular prop...

We have examined bacterial determinants that influence beta-lactam activity in Haemophilus influenzae cells cultivated in a system that reproduces in vivo growth conditions. Bacteria grown in diffusion chambers were recovered from the peritoneal cavities of rats, and their cell properties were compared with those of bacteria grown in broth cultures by various tests performed in vitro. The rate ...