Interaction of ceftobiprole with the low-affinity PBP 5 of Enterococcus faecium.
Ceftobiprole is a new cephalosporin that exhibits a high level of affinity for methicillin-resistant Staphylococcus aureus PBP 2a. It was reported that ceftobiprole did not interact with a mutated form of the low-affinity protein Enterococcus faecium PBP 5 (PBP 5fm) that, when overexpressed, confers a beta-lactam resistance phenotype to the bacterium. Our results show that ceftobiprole binds to unmutated PBP 5fm to form a stable acyl-enzyme and that ceftobiprole is able to efficiently kill a penicillin-resistant Enterococcus faecium strain that produces this protein.
Henry
Xavier
X
Centre d'Ingénierie des Protéines, Institut de Chimie B6a, Université de Liège, Sart Tilman, B-4000 Liège, Belgium.
Amoroso
Ana
A
Coyette
Jacques
J
Joris
Bernard
B
D000900:Anti-Bacterial Agents / Q000378:metabolism* / Q000494:pharmacology*; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D002511:Cephalosporins / Q000378:metabolism* / Q000494:pharmacology*; D016984:Enterococcus faecium / Q000187:drug effects* / Q000235:genetics / Q000378:metabolism*; D008826:Microbial Sensitivity Tests; D010400:Penicillin G / Q000494:pharmacology; D011485:Protein Binding / Q000235:genetics
D000900:Anti-Bacterial Agents; D001426:Bacterial Proteins; D002511:Cephalosporins; C443755:ceftobiprole; D010400:Penicillin G