Increase in glutamine-non-amidated muropeptides in the peptidoglycan of vancomycin-resistant Staphylococcus aureus strain Mu50
| Autor: | H Murakami, Hideaki Hanaki, N Kondo, Y Inaba, H Labischinski, Keiichi Hiramatsu |
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| Rok vydání: | 1998 |
| Předmět: |
Microbiology (medical)
Staphylococcus aureus Vancomycin-resistant Staphylococcus aureus Protein Conformation Glutamine Microbial Sensitivity Tests Peptidoglycan Biology medicine.disease_cause Microbiology Cell wall chemistry.chemical_compound Vancomycin medicine Pharmacology (medical) Amino Acids Antibacterial agent Pharmacology Drug Resistance Microbial medicine.disease biology.organism_classification Glycopeptide Infectious Diseases Phenotype chemistry Peptides Bacteria medicine.drug |
| Zdroj: | The Journal of antimicrobial chemotherapy. 42(3) |
| ISSN: | 0305-7453 |
| Popis: | The peptidoglycan compositions of vancomycin-resistant Staphylococcus aureus (VRSA) strain Mu50 (MIC 8 mg/L) and hetero-VRSA strain Mu3 (MIC 3 mg/L) were compared in order to understand the mechanism of vancomycin resistance. As compared with Mu3, the cell wall of Mu50 had increased amounts of glutamine-non-amidated muropeptides and decreased cross-linking of peptidoglycan with a greatly decreased dimer/monomer ratio of muropeptides. In agreement with this observation, the peptidoglycan of Mu50 bound 1.4 times more vancomycin than that of Mu3. The increase in non-amidated muropeptides and the reduced cross-linking of the cell-wall peptidoglycan may contribute to the vancomycin resistance by increasing the consumption of vancomycin by the pre-existing cell wall of Mu50 and reducing the amount of vancomycin reaching the cytoplasmic membrane where the vital targets of the antibiotic are situated. |
| Databáze: | OpenAIRE |
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