scholarly journals Competition of beta-lactam antibiotics for the penicillin-binding proteins of Pseudomonas aeruginosa, Enterobacter cloacae, Klebsiella aerogenes, Proteus rettgeri, and Escherichia coli: comparison with antibacterial activity and effects upon bacterial morphology.

1979 ◽  
Vol 16 (3) ◽  
pp. 325-328 ◽  
Author(s):  
N A Curtis ◽  
D Orr ◽  
G W Ross ◽  
M G Boulton
Keyword(s):  
Escherichia Coli ◽  
Pseudomonas Aeruginosa ◽  
Antibacterial Activity ◽  
Binding Proteins ◽  
Enterobacter Cloacae ◽  
Klebsiella Aerogenes ◽  
Beta Lactam ◽  
Penicillin Binding Proteins ◽  
Beta Lactam Antibiotics ◽  
Bacterial Morphology

scholarly journals Binding of Ceftobiprole and Comparators to the Penicillin-Binding Proteins of Escherichia coli, Pseudomonas aeruginosa, Staphylococcus aureus, and Streptococcus pneumoniae

2007 ◽  
Vol 51 (7) ◽  
pp. 2621-2624 ◽  
Author(s):  
Todd A. Davies ◽  
Malcolm G. P. Page ◽  
Wenchi Shang ◽  
Ted Andrew ◽  
Malgosia Kania ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Staphylococcus Aureus ◽  
Pseudomonas Aeruginosa ◽  
Antibacterial Activity ◽  
Streptococcus Pneumoniae ◽  
Binding Proteins ◽  
Tight Binding ◽  
Gram Negative ◽  
Penicillin Binding Proteins ◽  
Gram Positive Bacteria

ABSTRACT Ceftobiprole exhibited tight binding to PBP2a in methicillin-resistant Staphylococcus aureus, PBP2x in penicillin-resistant Streptococcus pneumoniae, and PBP3 and other essential penicillin-binding proteins in methicillin-susceptible S. aureus, Escherichia coli, and Pseudomonas aeruginosa. Ceftobiprole also bound well to PBP2 in the latter organisms, contributing to the broad-spectrum antibacterial activity against gram-negative and gram-positive bacteria.

scholarly journals Binding of 125I-labeled .BETA.-lactam antibiotics to the penicillin binding proteins of Escherichia coli.

1984 ◽  
Vol 37 (4) ◽  
pp. 389-393 ◽  
Author(s):  
FERNANDO ROJO ◽  
JUAN A. AYALA ◽  
ENRIQUE J. DE LA ROSA ◽  
MIGUEL A. DE PEDRO ◽  
VICENTE ARÁN ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Binding Proteins ◽  
Beta Lactam ◽  
Penicillin Binding Proteins ◽  
Beta Lactam Antibiotics

scholarly journals Effects of inhibitors of protein synthesis on lysis of Escherichia coli induced by beta-lactam antibiotics.

1996 ◽  
Vol 40 (4) ◽  
pp. 899-903 ◽  
Author(s):  
D G Rodionov ◽  
E E Ishiguro
Keyword(s):  
Escherichia Coli ◽  
Protein Synthesis ◽  
Binding Proteins ◽  
Rapid Development ◽  
Stringent Response ◽  
Beta Lactam ◽  
Penicillin Binding Proteins ◽  
Beta Lactam Antibiotics ◽  
Inhibition Of Protein Synthesis

The role of protein synthesis in ampicillin-induced lysis of Escherichia coli was investigated. The inhibition of protein synthesis through amino acid deprivation resulted in the rapid development of ampicillin tolerance as a consequence of the stringent response, as previously reported. In contrast, inhibition of protein synthesis by use of ribosome inhibitors such as chloramphenicol did not readily confer ampicillin tolerance and, in fact, promoted the development of both stages of the ampicillin-induced lysis process, i.e., (i) an ampicillin-dependent stage which apparently involves the interaction of penicillin-binding proteins with ampicillin and (ii) an ampicillin-independent stage which may represent the events leading to the deregulation of peptidoglycan hydrolase activity. We propose that lysis was facilitated when protein synthesis was inhibited because the production of new penicillin-binding proteins to replace those which were ampicillin inhibited was prevented under these conditions.

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