β-Lactam resistance development affects binding of penicillin-binding proteins (PBPs) of Clostridium perfringens to the fluorescent penicillin, BOCILLIN FL
| Autor: | John B. Sutherland, Fatemeh Rafii, Miseon Park |
|---|---|
| Rok vydání: | 2019 |
| Předmět: |
Penicillin binding proteins
Clostridium perfringens Mutant Penicillins medicine.disease_cause Real-Time Polymerase Chain Reaction Microbiology beta-Lactam Resistance 03 medical and health sciences chemistry.chemical_compound Bacterial Proteins Putative gene polycyclic compounds medicine Humans Penicillin-Binding Proteins 030304 developmental biology 0303 health sciences biology 030306 microbiology Chemistry Wild type Gene Expression Regulation Bacterial biochemical phenomena metabolism and nutrition Carboxypeptidase Anti-Bacterial Agents Penicillin Infectious Diseases Biochemistry biology.protein Clostridium Infections Peptidoglycan medicine.drug |
| Zdroj: | Anaerobe. 62 |
| ISSN: | 1095-8274 |
| Popis: | Alteration in the binding of bacterial penicillin-binding proteins (PBPs) to β-lactams is important in the development of drug resistance. The PBPs of wild type Clostridium perfringens ATCC 13124 and three β-lactam-resistant mutants were compared for the ability to bind to a fluorescent penicillin, BOCILLIN FL. The binding of the high molecular weight protein PBP1, a transpeptidase, to BOCILLIN FL was reduced in all of the resistant strains. In contrast, the binding of BOCILLIN FL to a low molecular weight protein, PBP6, a D-alanyl-d-alanine carboxypeptidase that was more abundant in all three resistant strains, was substantially increased. A competition assay with β-lactams reduced the binding of all of the PBPs, including PBP6, to BOCILLIN FL. β-Lactams enhanced transcription of the putative gene for PBP6 in both wild type and resistant strains. This is the first report showing that mutations in a high molecular weight PBP and overexpression of a low molecular weight PBP in resistant C. perfringens strains affected their binding to β-lactams. |
| Databáze: | OpenAIRE |
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