The stress-responsive Hsp90 chaperone is required for the production of the genotoxin colibactin and the siderophore yersiniabactin by Escherichia coli.

Christophe Garcie 1 Sophie Tronnet 2 Amélie Garénaux 3 Alex J Mccarthy 4 Alexander O Brachmann 5 Marie Pénary 2 Sébastien Houle 3 Jean-Philippe Nougayrède 2 Jörn Piel 5 Peter W Taylor 4 Charles M Dozois 3 Pierre Genevaux 2 Eric Oswald 1 Patricia Martin 1
1 Centre Hospitalier Universitaire de Toulouse - CHU Toulouse (FRANCE)
2 Université de Toulouse
3 INRS-IAF - Institut Armand Frappier
4 UCL - University College of London [London]
5 ETH Zürich - Eidgenössische Technische Hochschule [Zürich]
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
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Article dans une revue
Journal of Infectious Diseases, Oxford University Press (OUP), 2016, pp.Advance Access. 〈10.1093/infdis/jiw294 〉
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Contributeur : Michel Courcelles <>
Soumis le : mardi 2 août 2016 - 15:54:21
Dernière modification le : lundi 5 février 2018 - 15:22:10

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Christophe Garcie, Sophie Tronnet, Amélie Garénaux, Alex J Mccarthy, Alexander O Brachmann, et al.. 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, Oxford University Press (OUP), 2016, pp.Advance Access. 〈10.1093/infdis/jiw294 〉. 〈pasteur-01351061〉

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