Results 41 to 50 of about 400,542 (252)
Streptococcus pneumoniae and Neisseria meningitidis have very similar mechanisms of resistance to penicillin G. Although penicillin resistance is now common in S. pneumoniae, it is still rare in N. meningitidis.
L. Temime +3 more
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Penicillin-binding proteins in Borrelia burgdorferi [PDF]
Penicillin-binding proteins were identified in Borrelia burgdorferi membranes. A 94-kilodalton penicillin-binding protein was the first to be labeled with tritiated penicillin and was the first band to disappear in a competition experiment. Its binding ability was destroyed when membranes were preboiled. In addition, several of these penicillin-binding
C, Urban +4 more
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Resistance to β-lactam antibiotics conferred by point mutations in penicillin-binding proteins PBP3, PBP4 and PBP6 in Salmonella enterica. [PDF]
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
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Penicillin-binding proteins of Haemophilus ducreyi [PDF]
The penicillin-binding protein (PBP) profile of Haemophilus ducreyi was determined by a whole-cell-labeling assay. Only two major PBPs, of molecular weights 90,000 (PBP 1) and 38,500 (PBP 2), were detected in six of eight strains studied. Competition binding experiments and the attendant morphological effects suggested that PBP 1 was either a ...
B C, Lee, L E, Bryan
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The aminoacyltransferase MurM is an important penicillin resistance determinant in Streptococcus pneumoniae. This enzyme attaches a serine or alanine to the side chain of lysine, the third residue of the pentapeptide of lipid II, resulting in branched ...
Ragnhild Sødal Gjennestad +7 more
doaj +1 more source
Penicillin-binding proteins in Proteus species [PDF]
Penicillin-binding proteins in three species of Proteus, Proteus mirabilis, P. morganii, and P. rettgeri, were investigated by sodium dodecyl sulfate-polyacrylamide slab gel electrophoresis. Penicillin-binding proteins in these Proteus species were compared with those in Escherichia coli K-12.
S, Ohya +3 more
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Peptidoglycan (PG) is essential for bacterial survival and maintaining cell shape. The rod-shaped model bacterium Escherichia coli has a set of seven endopeptidases that remodel the PG during cell growth.
Jinglan Wang +4 more
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Subfamily-specific adaptations in the structures of two penicillin-binding proteins from Mycobacterium tuberculosis. [PDF]
Beta-lactam antibiotics target penicillin-binding proteins including several enzyme classes essential for bacterial cell-wall homeostasis. To better understand the functional and inhibitor-binding specificities of penicillin-binding proteins from the ...
Daniil M Prigozhin +8 more
doaj +1 more source
Penicillin-Binding Proteins and β-Lactam Resistance [PDF]
A number of ways and means have evolved to provide resistance to eubacteria challenged by beta-lactams. This review is focused on pathogens that resist by expressing low-affinity targets for these antibiotics, the penicillin-binding proteins (PBPs). Even within this narrow focus, a great variety of strategies have been uncovered such as the acquisition
Zapun, André +2 more
openaire +3 more sources
Non-Beta-Lactamase-Producing Penicillin-Resistant Enterococcus faecium in a Clinical Setting
Six clinical isolates of Enterococcus faecium highly resistant to penicillin are reported. These strains did not produce beta-lactamase and no plasmid DNA could be detected.
Daniel Eymard +6 more
doaj +1 more source

