Mode of action of ceftazidime: affinity for the penicillin-binding proteins of Escherichia coli K12, Pseudomonas aeruginosa and Staphylococcus aureus

1983 ◽  
Vol 12 (2) ◽  
pp. 119-126 ◽  
Author(s):  
Michael V. Hayes ◽  
David C. Orr
Keyword(s):  
Escherichia Coli ◽  
Staphylococcus Aureus ◽  
Pseudomonas Aeruginosa ◽  
Mode Of Action ◽  
Binding Proteins ◽  
Penicillin Binding Proteins ◽  
Escherichia Coli K12 ◽  
And Staphylococcus Aureus

scholarly journals Affinity of Tomopenem (CS-023) for Penicillin-Binding Proteins in Staphylococcus aureus, Escherichia coli, and Pseudomonas aeruginosa

2008 ◽  
Vol 53 (3) ◽  
pp. 1238-1241 ◽  
Author(s):  
Tetsufumi Koga ◽  
Chika Sugihara ◽  
Masayo Kakuta ◽  
Nobuhisa Masuda ◽  
Eiko Namba ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Staphylococcus Aureus ◽  
Pseudomonas Aeruginosa ◽  
Binding Proteins ◽  
Binding Protein ◽  
Penicillin Binding Protein ◽  
Penicillin Binding Proteins ◽  
E Coli ◽  
High Affinity

ABSTRACT Tomopenem (formerly CS-023), a novel 1β-methylcarbapenem, exhibited high affinity for penicillin-binding protein (PBP) 2 in Staphylococcus aureus, PBP 2 in Escherichia coli, and PBPs 2 and 3 in Pseudomonas aeruginosa, which are considered major lethal targets. Morphologically, tomopenem induced spherical forms in E. coli and short filamentation with bulges in P. aeruginosa, which correlated with the drug's PBP profiles. The potential of resistance of these bacteria to tomopenem was comparable to that to imipenem.

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.

Escherichia coli, Pseudomonas aeruginosa, and Staphylococcus aureus Attachment Patterns on Glass Surfaces with Nanoscale Roughness

2008 ◽  
Vol 58 (3) ◽  
pp. 268-273 ◽  
Author(s):  
Natasa Mitik-Dineva ◽  
James Wang ◽  
Vi Khanh Truong ◽  
Paul Stoddart ◽  
Francois Malherbe ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Staphylococcus Aureus ◽  
Pseudomonas Aeruginosa ◽  
Attachment Patterns ◽  
Glass Surfaces ◽  
And Staphylococcus Aureus ◽  
Nanoscale Roughness
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