Impact of chlorhexidine digluconate and temperature on curli production in Escherichia coli—consequence on its adhesion ability
| Autor: | Laurence Mora, Ali Othmane, Laurent Coquet, Julie Hardouin, Thierry Jouenne, Antoine Obry, Nabil Borghol |
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| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Microbiology (medical) biology Chemistry 030106 microbiology Mutant Biofilm Periplasmic space Adhesion medicine.disease_cause biology.organism_classification Microbiology 3. Good health 03 medical and health sciences 030104 developmental biology medicine Protein folding Bacterial outer membrane Escherichia coli Bacteria |
| Zdroj: | AIMS Microbiology. 3:915-937 |
| ISSN: | 2471-1888 |
| Popis: | Chlorhexidine-Digluconate (CHX-Dg) is a biocide widely used as disinfectant or antiseptic in clinical and domestic fields. It is often found in the formulation of solutions to treat superficial wounds. Nevertheless, few studies have focused on its effects on Escherichia coli while this bacterium is commonly involved in mixed infections. Therefore, the impact of CHX-Dg and temperature on E. coli was investigated; particularly the curli production. In accordance with bibliographic data, the curli production decreased when the temperature of the culture was shift from 30 °C to 37 °C. The bacterial adhesion to abiotic surfaces was also reduced. Surprisingly, the curli production at 37 °C was maintained in presence of antiseptic and the bacterial adhesion was improved at a very low concentration (1 µg ml−1) of CHX-Dg. Complementary investigations with a cpxR mutant demonstrated that the CpxA/R-TCS (Two-Component System) is involved in the temperature-dependent control of the curli expression. Indeed, the curli production was not altered by the growth temperature in the mutant. Otherwise, no relationship between CHX-Dg and the Cpx-TCS was shown. A subsequent proteomic investigation revealed the alteration of the production of 44 periplasmic and outer membrane proteins in presence of CHX-Dg. These proteins are involved in the transport of small molecules, the envelope integrity, the stress response as well as the protein folding. |
| Databáze: | OpenAIRE |
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