Impact of chlorhexidine digluconate and temperature on curli production in <em>Escherichia coli</em>—consequence on its adhesion ability

Laurent Coquet; Antoine Obry; Nabil Borghol; Julie Hardouin; Laurence Mora; Ali Othmane; Thierry Jouenne; Laurent Coquet; Antoine Obry; Nabil Borghol; Julie Hardouin; Laurence Mora; Ali Othmane; Thierry Jouenne

doi:10.3934/microbiol.2017.4.915

AIMS Microbiology

2017, Volume 3, Issue 4: 915-937. doi: 10.3934/microbiol.2017.4.915

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Research article

Impact of chlorhexidine digluconate and temperature on curli production in Escherichia coli—consequence on its adhesion ability

1.
CNRS UMR6270, Normandie University, UNIROUEN, Plate-forme PISSARO, Mont-Saint-Aignan, France
2.
INSERM U905, Normandie University, UNIROUEN, Plate-forme PISSARO, France
3.
Biophysical Laboratory, Faculty of Medicine of Monastir, Monastir, Tunisia
4.
INSERM U1148, Laboratory for Vascular Transitional Sciences, Galileo Institute, Paris 13 University, Sorbonne Paris Cité, Villetaneuse, France

Received: 06 July 2017 Accepted: 27 November 2017 Published: 01 December 2017

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.
- biofilm,
- chlorhexidine,
- curli,
- Escherichia coli,
- outer membrane,
- proteome,
- Cpx-TCS
Citation: Laurent Coquet, Antoine Obry, Nabil Borghol, Julie Hardouin, Laurence Mora, Ali Othmane, Thierry Jouenne. Impact of chlorhexidine digluconate and temperature on curli production in Escherichia coli—consequence on its adhesion ability[J]. AIMS Microbiology, 2017, 3(4): 915-937. doi: 10.3934/microbiol.2017.4.915

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Abstract

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.

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