The penicillin binding proteins (PBPs) that in Streptococcus faecium are the targets for inhibitory activity of beta-lactam antibiotics were analyzed both in cells growing at their fastest and at reduced rates. It was found that while under the former conditions the PBPs showed the highest affinity for penicillin, under the latter the target is shifted to PBP (PBP5) that has a very low affinity for penicillin and other beta-lactams. The possibility that conditions met by Enterococci in human infections cause a shifting of the penicillin target and the possible role of such shifting in resistance to beta-lactams during therapy are discussed
Streptococcus pneumoniae is an important human pathogen, causing about 100 millions of cases of dise...
AbstractMethidllin-resistant clinical isolates of Staphylococcus aureus are intrinsically resistant ...
The effects of variations in growth conditions on the penicillin response of Streptococcus faecium A...
Enterococci are characterized by an intrinsic resistance to growth inhibition by beta-lactam antibio...
The mode of bacterial killing by penicillins is still unknown in spite of many studies on the subjec...
Two mechanisms are responsible for resistance of enterococci to beta-lactam antibiotics: alterations...
Penicillin-binding protein (PBP) 5 of Streptococcus faecium has been shown to have a very low affini...
The MICs and MBCs of benzylpenicillin, ampicillin, cefotaxime, and methicillin were evaluated agains...
Enterococci are characterized by an intrinsic resistance to growth inhibition by p-Iactam antibi-oti...
Penicillin-binding proteins (PBPs) are enzymes responsible for the polymerization of the glycan stra...
Beta-lactam antibiotics sensitize Enterococcus faecium to killing by endogenous antimicrobial peptid...
By challenging the efficiency of some of our most useful antimicrobial weapons, bacterial antibiotic...
Binding affinity of penicillin-binding proteins (PBP) of Staphylococcus aureus for several {3-lactam...
It has long been recognized that the modification of penicillin-binding proteins (PBPs) to reduce th...
peer reviewedWith the help of a new highly sensitive method allowing the quantification of free peni...
Streptococcus pneumoniae is an important human pathogen, causing about 100 millions of cases of dise...
AbstractMethidllin-resistant clinical isolates of Staphylococcus aureus are intrinsically resistant ...
The effects of variations in growth conditions on the penicillin response of Streptococcus faecium A...
Enterococci are characterized by an intrinsic resistance to growth inhibition by beta-lactam antibio...
The mode of bacterial killing by penicillins is still unknown in spite of many studies on the subjec...
Two mechanisms are responsible for resistance of enterococci to beta-lactam antibiotics: alterations...
Penicillin-binding protein (PBP) 5 of Streptococcus faecium has been shown to have a very low affini...
The MICs and MBCs of benzylpenicillin, ampicillin, cefotaxime, and methicillin were evaluated agains...
Enterococci are characterized by an intrinsic resistance to growth inhibition by p-Iactam antibi-oti...
Penicillin-binding proteins (PBPs) are enzymes responsible for the polymerization of the glycan stra...
Beta-lactam antibiotics sensitize Enterococcus faecium to killing by endogenous antimicrobial peptid...
By challenging the efficiency of some of our most useful antimicrobial weapons, bacterial antibiotic...
Binding affinity of penicillin-binding proteins (PBP) of Staphylococcus aureus for several {3-lactam...
It has long been recognized that the modification of penicillin-binding proteins (PBPs) to reduce th...
peer reviewedWith the help of a new highly sensitive method allowing the quantification of free peni...
Streptococcus pneumoniae is an important human pathogen, causing about 100 millions of cases of dise...
AbstractMethidllin-resistant clinical isolates of Staphylococcus aureus are intrinsically resistant ...
The effects of variations in growth conditions on the penicillin response of Streptococcus faecium A...