Inactivation of ahpC renders Stenotrophomonas maltophilia resistant to the disinfectant hydrogen peroxide
| Autor: | Jurairat Chittrakanwong, Skorn Mongkolsuk, Paiboon Vattanaviboon, Nisanart Charoenlap, Luksika Jiramonai, Naruemon Tunsakul |
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| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Stenotrophomonas maltophilia 030106 microbiology Mutant Mutagenesis (molecular biology technique) Reductase Microbiology 03 medical and health sciences Plasmid Bacterial Proteins Drug Resistance Bacterial Gene Silencing Molecular Biology biology Chemistry Gene Expression Regulation Bacterial Hydrogen Peroxide Peroxiredoxins General Medicine biology.organism_classification 030104 developmental biology Catalase biology.protein Bacteria Disinfectants Cysteine |
| Zdroj: | Antonie van Leeuwenhoek. 112:809-814 |
| ISSN: | 1572-9699 0003-6072 |
| DOI: | 10.1007/s10482-018-1203-9 |
| Popis: | Inactivation of ahpC, encoding alkyl hydroperoxide reductase, rendered Stenotrophomonas maltophilia more resistant to H2O2; the phenotype was directly correlated with enhanced total catalase activity, resulting from an increased level of KatA catalase. Plasmid-borne expression of ahpC from pAhpCsm could complement all of the mutant phenotypes. Mutagenesis of the proposed AhpC peroxidactic and resolving cysteine residues to alanine (C47A and C166A) on the pAhpCsm plasmid diminished its ability to complement the ahpC mutant phenotypes, suggesting that the mutagenized ahpC was non-functional. As mutations commonly occur in bacteria living in hostile environment, our data suggest that point mutations in ahpC at codons required for the enzyme function (such as C47 and C166), the AhpC will be non-functional, leading to high resistance to the disinfectant H2O2. |
| Databáze: | OpenAIRE |
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