Kinetics of penicillin binding to penicillin-binding proteins of Staphylococcus aureus
| Autor: | Henry F. Chambers, C J Hackbarth, Meena Sachdeva |
|---|---|
| Rok vydání: | 1994 |
| Předmět: |
Staphylococcus aureus
Penicillin binding proteins Penicillin Resistance Penicillins Muramoylpentapeptide Carboxypeptidase medicine.disease_cause Binding Competitive Biochemistry Microbiology Muramoylpentapeptide carboxypeptidase Antibiotic resistance Bacterial Proteins polycyclic compounds medicine Penicillin-Binding Proteins Molecular Biology Antibacterial agent biology Membrane Proteins Cell Biology biochemical phenomena metabolism and nutrition biology.organism_classification Penicillin Kinetics Hexosyltransferases Peptidyl Transferases bacteria Penicillin binding Carrier Proteins Bacteria Research Article Protein Binding medicine.drug |
| Zdroj: | Biochemical Journal. 301:139-144 |
| ISSN: | 1470-8728 0264-6021 |
| Popis: | Reduced affinity of penicillin-binding proteins (PBPs) for binding penicillin has been proposed as a mechanism of beta-lactam antibiotic resistance in staphylococci. Penicillin binding by PBPs of three penicillin-susceptible and two penicillin-resistant strains of Staphylococcus aureus was studied in kinetic assays to determine rate constants, drug concentrations at which PBPs were bound and the relationship between concentrations that bound PBPs and concentrations that inhibited bacterial growth. PBPs 1 and 2 of the resistant strains exhibited slower acylation and more rapid deacylation than susceptible strains. In contrast PBP 4, a naturally low-affinity PBP, was modified such that it exhibited a lower rate of deacylation. The concentrations of penicillin at which modified PBPs were bound correlated with concentrations that inhibited growth of the resistant strains. Acquisition of penicillin resistance in these strains of S. aureus results, at least in part, from structural modifications affecting binding of multiple PBPs and appears to include recruitment of a non-essential PBP, PBP 4. |
| Databáze: | OpenAIRE |
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