scholarly journals Coagulase-negative staphylococci resistant to beta-lactam antibiotics in vivo produce penicillin-binding protein 2a.

1987 ◽  
Vol 31 (12) ◽  
pp. 1919-1924 ◽  
Author(s):  
H F Chambers
Keyword(s):  
Binding Protein ◽  
Penicillin Binding Protein ◽  
Beta Lactam ◽  
Coagulase Negative Staphylococci ◽  
Beta Lactam Antibiotics

scholarly journals Penicillin-binding protein 2x of Streptococcus pneumoniae: enzymic activities and interactions with β-lactams

1993 ◽  
Vol 292 (3) ◽  
pp. 735-741 ◽  
Author(s):  
M Jamin ◽  
C Damblon ◽  
S Millier ◽  
R Hakenbeck ◽  
J M Frère
Keyword(s):  
Streptococcus Pneumoniae ◽  
Extracellular Enzymes ◽  
Binding Protein ◽  
Soluble Form ◽  
Penicillin Binding Protein ◽  
Beta Lactam ◽  
Easy Method ◽  
Beta Lactam Antibiotics ◽  
Catalytic Behaviour ◽  
First Time

The high-molecular-mass penicillin-binding protein (PBP) 2x, one of the primary targets of beta-lactam antibiotics in Streptococcus pneumoniae, has been produced as a soluble form and purified in large amounts. It has been shown to catalyse hydrolysis and transfer reactions with different ester and thiolester substrates and its catalytic behaviour was often similar to that of the soluble DD-peptidase from Streptomyces R61. This provided an easy method to monitor the activity of the PBP. For the first time, a reliable kinetic study of the interaction between a lethal target and beta-lactam antibiotics has been performed. Characteristic kinetic parameters were obtained with different beta-lactam compounds. These results not only validated the mechanism established with non-essential extracellular enzymes, but will also constitute the basis for comparative studies of the low-affinity variants from penicillin-resistant strains.

scholarly journals Susceptibility to beta-lactam antibiotics of Pseudomonas aeruginosa overproducing penicillin-binding protein 3.

1997 ◽  
Vol 41 (5) ◽  
pp. 1158-1161 ◽  
Author(s):  
X Liao ◽  
R E Hancock
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Binding Protein ◽  
Broad Host Range ◽  
Penicillin Binding Protein ◽  
Beta Lactam ◽  
Beta Lactams ◽  
E Coli ◽  
Beta Lactam Antibiotics ◽  
Range Vector ◽  
Cell Inhibition

By using a broad-host-range vector, pUCP27, the Pseudomonas aeruginosa and Escherichia coli pbpB genes, which encode penicillin-binding protein 3 (PBP3), were separately overexpressed in a P. aeruginosa strain, PAO4089, that is deficient in producing chromosomal beta-lactamase. Susceptibility studies indicated that overproduction of the P. aeruginosa PBP3 in PAO4089 resulted in twofold-increased resistance to aztreonam, fourfold-increased resistance to cefepime and cefsulodin, and eightfold-increased resistance to ceftazidime, whereas overproduction of the P. aeruginosa PBP3 in PAO4089 did not affect susceptibility to PBP1-targeted cephaloridine or PBP2-targeted imipenem. Similar results were obtained with PAO4089 overproducing E. coli PBP3, with the exception that there was no influence on the MICs or minimal bactericidal concentrations of cefsulodin and cefepime, which have very low affinities for E. coli PBP3. These data are consistent with the conclusion that PBP3 has to achieve a certain level of saturation, with beta-lactams targeted to this protein, to result in cell inhibition or death.

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