Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 287, Issue 38, Pages 32096-32102Publisher
ELSEVIER
DOI: 10.1074/jbc.M112.355644
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Funding
- Canadian Institutes of Health Research
- Howard Hughes Medical Institute
- Michael Smith Foundation of Health Research
- Canada Foundation for Innovation
- Royal Society
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Methicillin-resistant Staphylococcus aureus (MRSA) is an antibiotic-resistant strain of S. aureus afflicting hospitals and communities worldwide. Of greatest concern is its development of resistance to current last-line-of-defense antibiotics; new therapeutics are urgently needed to combat this pathogen. Ceftobiprole is a recently developed, latest generation cephalosporin and has been the first to show activity against MRSA by inhibiting essential peptidoglycan transpeptidases, including the beta-lactam resistance determinant PBP2a, from MRSA. Here we present the structure of the complex of ceftobiprole bound to PBP2a. This structure provides the first look at the molecular details of an effective beta-lactam-resistant PBP interaction, leading to new insights into the mechanism of ceftobiprole efficacy against MRSA.
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