Garcie, C;
Tronnet, S;
Garénaux, A;
McCarthy, AJ;
Brachmann, AO;
Pénary, M;
Houle, S;
... Martin, P; + view all
(2016)
The stress-responsive Hsp90 chaperone is required for the production of the genotoxin colibactin and the siderophore yersiniabactin by Escherichia coli.
Journal of Infectious Diseases
, 214
(6)
pp. 916-924.
10.1093/infdis/jiw294.
Preview |
Text
JID 2016.pdf - Accepted Version Download (1MB) | Preview |
Abstract
The genotoxin colibactin synthesized by Escherichia coli is a secondary metabolite belonging to the chemical family of hybrid polyketide/non-ribosomal peptide compounds. It is produced by a complex biosynthetic assembly line encoded by the pks pathogenicity island. The presence of this large cluster of genes in the E. coli genome is invariably associated with the High-Pathogenicity Island, encoding the siderophore yersiniabactin that belongs to the same chemical family as colibactin. The E. coli heat shock protein HtpG (Hsp90Ec) is the bacterial homolog of the eukaryotic molecular chaperone Hsp90 involved in the protection of cellular proteins against a variety of environmental stresses. In contrast to the eukaryotic Hsp90, the functions and client proteins of Hsp90Ec are poorly known. Here, we demonstrated that production of colibactin and yersiniabactin is abolished in the absence of Hsp90Ec We further characterized an interplay between the Hsp90Ec molecular chaperone and the ClpQ protease involved in colibactin and yersiniabactin synthesis. Finally, we demonstrated that Hsp90Ec is required for the full in vivo virulence of extraintestinal pathogenic E. coli This is the first report highlighting the role of heat shock protein Hps90Ec in the production of two secondary metabolites involved in E. coli virulence.
| Type: | Article |
|---|---|
| Title: | The stress-responsive Hsp90 chaperone is required for the production of the genotoxin colibactin and the siderophore yersiniabactin by Escherichia coli |
| Open access status: | An open access version is available from UCL Discovery |
| DOI: | 10.1093/infdis/jiw294 |
| Publisher version: | http://dx.doi.org/10.1093/infdis/jiw294 |
| Language: | English |
| Additional information: | Copyright © The Author 2016. Published by Oxford University Press for the Infectious Diseases Society of America. All rights reserved. This is a pre-copyedited, author-produced PDF of an article accepted for publication in the Journal of Infectious Diseases following peer review. The version of record [Garcie, C; Tronnet, S; Garénaux, A; McCarthy, AJ; Brachmann, AO; Pénary, M; Houle, S; (2016) The stress-responsive Hsp90 chaperone is required for the production of the genotoxin colibactin and the siderophore yersiniabactin by Escherichia coli. Journal of Infectious Diseases, 214 (6) pp. 916-924. 10.1093/infdis/jiw294] is available online at: http://dx.doi.org/10.1093/infdis/jiw294 |
| Keywords: | heat shock proteins, Hsp90, HtpG, stress response, colibactin, yersiniabactin, siderophores, virulence, meningitis, Escherichia coli |
| UCL classification: | UCL UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > UCL School of Pharmacy UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > UCL School of Pharmacy > Pharmaceutics |
| URI: | https://discovery.ucl.ac.uk/id/eprint/1503878 |
Archive Staff Only
 |
View Item |
