title: The opgC gene is required for OPGs succinylation and is osmoregulated through RcsCDB and EnvZ/OmpR in the phytopathogen Dickeya dadantii.
abstract: Osmoregulated periplasmic glucans (OPGs) are a family of periplasmic oligosaccharides found in the envelope of most Proteobacteria. They are required for virulence of zoo- and phyto-pathogens. The glucose backbone of OPGs is substituted by various kinds of molecules depending on the species, O-succinyl residues being the most widely distributed. In our model, Dickeya dadantii, a phytopathogenic bacteria causing soft rot disease in a wide range of plant species, the backbone of OPGs is substituted by O-succinyl residues in media of high osmolarity and by O-acetyl residues whatever the osmolarity. The opgC gene encoding a transmembrane protein required for the succinylation of the OPGs in D. dadantii was found after an in silico search of a gene encoding a protein with the main characteristics recovered in the two previously characterized OpgC of E. coli and R. sphaeroides, i.e. 10 transmembrane segments and one acyl-transferase domain. Characterization of the opgC gene revealed that high osmolarity expression of the succinyl transferase is controlled by both the EnvZ-OmpR and RcsCDB phosphorelay systems. The loss of O-succinyl residue did not affect the virulence of D. dadantii, suggesting that only the glucose backbone of OPGs is required for virulence.
authors.affiliation: Structural and Functional Glycobiology Unit, UMR CNRS-Lille1 8576, University of Lille, 59655 Villeneuve d'Ascq cedex, France.
authors.forename: Sébastien
authors.initials: S
authors.lastname: Bontemps-Gallo
authors.affiliation: Structural and Functional Glycobiology Unit, UMR CNRS-Lille1 8576, University of Lille, 59655 Villeneuve d'Ascq cedex, France.
authors.forename: Edwige
authors.initials: E
authors.lastname: Madec
authors.affiliation: Structural and Functional Glycobiology Unit, UMR CNRS-Lille1 8576, University of Lille, 59655 Villeneuve d'Ascq cedex, France.
authors.forename: Catherine
authors.initials: C
authors.lastname: Robbe-Masselot
authors.affiliation: Center for Human Genetics, University of Leuven, Herestraat 49, 3000 Leuven, Belgium.
authors.forename: Erika
authors.initials: E
authors.lastname: Souche
authors.affiliation: Structural and Functional Glycobiology Unit, UMR CNRS-Lille1 8576, University of Lille, 59655 Villeneuve d'Ascq cedex, France.
authors.forename: Jacqueline
authors.initials: J
authors.lastname: Dondeyne
authors.affiliation: Structural and Functional Glycobiology Unit, UMR CNRS-Lille1 8576, University of Lille, 59655 Villeneuve d'Ascq cedex, France.
authors.forename: Jean-Marie
authors.initials: JM
authors.lastname: Lacroix
mesh_terms: D001426:Bacterial Proteins / Q000235:genetics* / Q000378:metabolism; D004755:Enterobacteriaceae / Q000235:genetics* / Q000378:metabolism*; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D023061:Gene Order; D005816:Genetic Complementation Test; D016680:Genome, Bacterial; D005936:Glucans / Q000378:metabolism*; D009994:Osmolar Concentration; D064587:Osmoregulation; D019897:Periplasm / Q000378:metabolism*; D010766:Phosphorylation; D011401:Promoter Regions, Genetic; D011485:Protein Binding; D014774:Virulence / Q000235:genetics
chemical_list: D001426:Bacterial Proteins; D005936:Glucans