Interaction of ceftobiprole with the low-affinity PBP 5 of Enterococcus faecium.

Antimicrobial Agents and Chemotherapy
Xavier HenryBernard Joris

Abstract

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.

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Citations

Mar 28, 2012·Antimicrobial Agents and Chemotherapy·Kavindra V Singh, Barbara E Murray
Sep 26, 2013·Antimicrobial Agents and Chemotherapy·Xavier HenryBernard Joris
Nov 18, 2015·Future Microbiology·Thomas W L Scheeren
Jan 28, 2016·Protein Science : a Publication of the Protein Society·Dustin T KingNatalie C J Strynadka
May 8, 2013·European Journal of Medicinal Chemistry·Georges DiveJacqueline Marchand-Brynaert
Oct 5, 2010·Current Opinion in Microbiology·Leticia I LlarrullShahriar Mobashery
Jun 30, 2015·Future Microbiology·J M PericásJ M Miró
Oct 19, 2012·Virulence·Brian L Hollenbeck, Louis B Rice
Oct 12, 2014·The Journal of Antimicrobial Chemotherapy·Brian J WerthMichael J Rybak
Jul 19, 2016·World Journal of Emergency Surgery : WJES·Massimo SartelliPerluigi Viale
Dec 3, 2014·Current Opinion in Pharmacology·Jean-Marie Frère, Malcolm G P Page
Dec 25, 2013·Antimicrobial Agents and Chemotherapy·George SakoulasVictor Nizet

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