The competition of α-sulfocephalosporins for the penicillin-binding proteins of Escherichia coli K12 and Pseudomonas aeruginosa—comparison with effects upon morphology

1980 ◽  
Vol 6 (2) ◽  
pp. 189-196 ◽  
Author(s):  
Nigel A. C. Curtis ◽  
Michael G. Boulton ◽  
David Orr ◽  
Gordon W. Ross
Keyword(s):  
Escherichia Coli ◽  
Pseudomonas Aeruginosa ◽  
Binding Proteins ◽  
Penicillin Binding Proteins ◽  
Escherichia Coli K12

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 A novel character of acylaminobenzylpenicillin apalcillin, in binding to penicillin-binding proteins of Escherichia coli and Pseudomonas aeruginosa.

1984 ◽  
Vol 37 (3) ◽  
pp. 293-296
Author(s):  
MASATOMO FUKASAWA ◽  
HIROSHI NOGUCHI ◽  
SUSUMU MITSUHASHI ◽  
FUMITOSHI ISHINO ◽  
MICHIO MATSUHASHI ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Pseudomonas Aeruginosa ◽  
Binding Proteins ◽  
Penicillin Binding Proteins

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 Affinity of Doripenem and Comparators to Penicillin-Binding Proteins in Escherichia coli and Pseudomonas aeruginosa

2008 ◽  
Vol 52 (4) ◽  
pp. 1510-1512 ◽  
Author(s):  
Todd A. Davies ◽  
Wenchi Shang ◽  
Karen Bush ◽  
Robert K. Flamm
Keyword(s):  
Escherichia Coli ◽  
Pseudomonas Aeruginosa ◽  
Cell Death ◽  
Broad Spectrum ◽  
Binding Proteins ◽  
Penicillin Binding Protein ◽  
Gram Negative ◽  
Penicillin Binding Proteins ◽  
High Affinity ◽  
Affinity Profile

ABSTRACT Doripenem, a parenteral carbapenem, exhibited high affinity for penicillin-binding protein 2 (PBP2) and PBP3 in Pseudomonas aeruginosa and PBP2 in Escherichia coli, the primary PBPs whose inhibition leads to cell death. This PBP affinity profile correlates with the broad-spectrum gram-negative activity observed with doripenem.

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