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Pathogens 2018, 7(4), 95; https://doi.org/10.3390/pathogens7040095

Epigallocatechin Gallate Remodelling of Hfq Amyloid-Like Region Affects Escherichia coli Survival

1
Laboratoire Léon Brillouin LLB, CEA, CNRS UMR12, Université Paris Saclay, CEA Saclay, 91191 Gif-sur-Yvette, France
2
Synchrotron SOLEIL, L’Orme des Merisiers, Saint Aubin BP48, 91192, Gif-sur-Yvette, France
3
Institut Curie, INSERM U1196, and CNRS UMR9187, 91405 Orsay Cedex, France
4
UFR SDV, Université Paris Diderot, Sorbonne Paris Cité, 75013 Paris, France
*
Authors to whom correspondence should be addressed.
Received: 11 November 2018 / Revised: 22 November 2018 / Accepted: 26 November 2018 / Published: 1 December 2018
(This article belongs to the Special Issue Inactivate Bacterial Resistance Mechanisms)
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Abstract

Hfq is a pleiotropic regulator that has key roles in the control of genetic expression. The protein noticeably regulates translation efficiency and RNA decay in Gram-negative bacteria, due to the Hfq-mediated interaction between small regulatory noncoding RNA and mRNA. This property is of primary importance for bacterial adaptation and virulence. We have previously shown that the Hfq E. coli protein, and more precisely its C-terminal region (CTR), self-assembles into an amyloid-like structure. In the present work, we demonstrate that epigallocatechin gallate (EGCG), a major green tea polyphenol compound, targets the Hfq amyloid region and can be used as a potential antibacterial agent. We analysed the effect of this compound on Hfq amyloid fibril stability and show that EGCG both disrupts Hfq-CTR fibrils and inhibits their formation. We show that, even if EGCG affects other bacterial amyloids, it also specifically targets Hfq-CTR in vivo. Our results provide an alternative approach for the utilisation of EGCG that may be used synergistically with conventional antibiotics to block bacterial adaptation and treat infections. View Full-Text
Keywords: bacterial amyloid; functional amyloid; protein fibrils; epigallocatechin gallate (EGCG); protein fibrillation inhibition; Hfq; bacterial adaptation; antibacterial bacterial amyloid; functional amyloid; protein fibrils; epigallocatechin gallate (EGCG); protein fibrillation inhibition; Hfq; bacterial adaptation; antibacterial
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).

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    Description: Sup Figure S1: DSC analysis of Hfq CTR11 melting. Thermal analysis was carried out with a TA Instruments DSC Q100 differential scanning calorimeter at 2K/min from 20 to 135°C. The onset temperature (63.95°C) is considered to be the equivalent of Tm measured by SRCD
  • Externally hosted supplementary file 2
    Link: https://www.mdpi.com/xxx/s2
    Description: Sup Figure S2: Hfq-CTR11/EGCG equilibrium dissociation constant measurement using Isothermal titration calorimetry (MALVERN PEAQ-ITC).
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Partouche, D.; Turbant, F.; El Hamoui, O.; Campidelli, C.; Bombled, M.; Trépout, S.; Wien, F.; Arluison, V. Epigallocatechin Gallate Remodelling of Hfq Amyloid-Like Region Affects Escherichia coli Survival. Pathogens 2018, 7, 95.

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