Spontaneous Nisin-ResistantListeria monocytogenesMutants with Increased Expression of a Putative Penicillin-Binding Protein and Their Sensitivity to Various Antibiotics
| Autor: | Frank Møller Aarestrup, Susanne Knøchel, Karen Sørensen, Anne Gravesen |
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| Rok vydání: | 2001 |
| Předmět: |
DNA
Bacterial Microbiology (medical) Penicillin binding proteins Immunology Mutant Microbial Sensitivity Tests Muramoylpentapeptide Carboxypeptidase Biology Microbiology chemistry.chemical_compound Bacterial Proteins Bacteriocin Gene expression polycyclic compounds Penicillin-Binding Proteins Nisin Pharmacology Reverse Transcriptase Polymerase Chain Reaction Drug Resistance Microbial biochemical phenomena metabolism and nutrition Lantibiotics Blotting Northern Biopreservation Lipids Listeria monocytogenes Anti-Bacterial Agents Hexosyltransferases chemistry Biochemistry Mutation Peptidyl Transferases bacteria Carrier Proteins CLPB Polymorphism Restriction Fragment Length |
| Zdroj: | Microbial Drug Resistance. 7:127-135 |
| ISSN: | 1931-8448 1076-6294 |
| Popis: | A concern regarding the use of bacteriocins, as for example the lantibiotic nisin, for biopreservation of certain food products is the possibility of resistance development and potential cross-resistance to antibiotics in the target organism. The genetic basis for nisin resistance development is as yet unknown. We analyzed changes in gene expression following nisin resistance development in Listeria monocytogenes 412 by restriction fragment differential display. The mutant had increased expression of a protein with strong homology to the glycosyltransferase domain of high-molecular-weight penicillin-binding proteins (PBPs), a histidine protein kinase, a protein of unknown function, and ClpB (putative functions from homology). The three former proteins had increased expression in a total of six out of 10 independent mutants originating from five different wild-type strains, indicating a prevalent nisin resistance mechanism under the employed isolation conditions. Increased expression of the putative PBP may affect the cell wall composition and thereby alter the sensitivity to cell wall-targeting compounds. The mutants had an isolate-specific increase in sensitivity to different beta-lactams and a slight decrease in sensitivity to another lantibiotic, mersacidin. A model incorporating these observations is proposed based on current knowledge of nisin's mode of action. |
| Databáze: | OpenAIRE |
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