Differential Inhibition of Staphylococcus aureus PBP2 by Glycopeptide Antibiotics
| Autor: | Gianbattista Panzone, Markus Oberthür, Catherine Leimkuhler, Dianah Barrett, Daniel Kahne, Brian Falcone, Suzanne Walker, Lan Chen, Binyuan Sun, Stefano Donadio |
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| Rok vydání: | 2005 |
| Předmět: |
Staphylococcus aureus
Penicillin binding proteins medicine.drug_class Antibiotics Microbial Sensitivity Tests medicine.disease_cause Biochemistry Catalysis Bacterial cell structure Substrate Specificity chemistry.chemical_compound Colloid and Surface Chemistry Vancomycin medicine Penicillin-Binding Proteins Antibacterial agent Dipeptides General Chemistry Uridine Diphosphate N-Acetylmuramic Acid Glycopeptide Anti-Bacterial Agents Kinetics chemistry Peptidoglycan medicine.drug |
| Zdroj: | Journal of the American Chemical Society. 127:3250-3251 |
| ISSN: | 1520-5126 0002-7863 |
| Popis: | The glycopeptide antibiotics prevent maturation of the bacterial cell wall by binding to the terminal d-alanyl-d-alanine moiety of peptidoglycan precursors, thereby inhibiting the enzymes involved in the final stages of peptidoglycan synthesis. However, there are significant differences in the biological activity of particular glycopeptide derivatives that are not related to their affinity for d-Ala-d-Ala. We compare the ability of vancomycin and a set of clinically relevant glycopeptides to inhibit Staphylococcus aureus PBP2 (penicillin binding protein), the major transglycosylase in a clinically relevant pathogen, S. aureus. We report experiments suggesting that activity differences between glycopeptides against this organism reflect a combination of substrate binding and secondary interactions with key enzymes involved in peptidoglycan synthesis. |
| Databáze: | OpenAIRE |
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