title: Proteomic analysis of a non-virulent mutant of the phytopathogenic bacterium Erwinia chrysanthemi deficient in osmoregulated periplasmic glucans: change in protein expression is not restricted to the envelope, but affects general metabolism.
abstract: Osmoregulated periplasmic glucans (OPGs) are general constituents of the envelope of Gram-negative bacteria. They are required for full virulence of bacterial phytopathogens such as Pseudomonas syringae, Xanthomonas campestris and Erwinia chrysanthemi. E. chrysanthemi is a pectinolytic gamma-proteobacterium that causes soft rot disease on a wide range of plant species. In addition to the loss of virulence, opg mutants exhibit a pleiotropic phenotype that affects motility, bile-salt resistance, exoenzyme secretion, exopolysaccharide synthesis and membrane lipid composition. This is believed to be the first proteomic analysis of an OPG-defective mutant of E. chrysanthemi and it revealed that, in addition to the effects described, catabolic enzyme synthesis was enhanced and there was a greater abundance of some proteins catalysing the folding and degradation of proteins needed for various stress responses. Thus, in the opg mutant strain, loss of virulence was the result of a combination of envelope structure changes and cellular metabolism modifications.
authors.affiliation: Unité de Glycobiologie Structurale et Fonctionnelle, UMR USTL-CNRS 8576 IFR 118, Université des Sciences et Technologies de Lille, 59655 Villeneuve d'Ascq Cedex, France.
authors.forename: Franck
authors.initials: F
authors.lastname: Bouchart
authors.affiliation: Unité de Glycobiologie Structurale et Fonctionnelle, UMR USTL-CNRS 8576 IFR 118, Université des Sciences et Technologies de Lille, 59655 Villeneuve d'Ascq Cedex, France.
authors.forename: Aurélie
authors.initials: A
authors.lastname: Delangle
authors.affiliation: Unité de Glycobiologie Structurale et Fonctionnelle, UMR USTL-CNRS 8576 IFR 118, Université des Sciences et Technologies de Lille, 59655 Villeneuve d'Ascq Cedex, France.
authors.forename: Jérôme
authors.initials: J
authors.lastname: Lemoine
authors.affiliation: Unité de Glycobiologie Structurale et Fonctionnelle, UMR USTL-CNRS 8576 IFR 118, Université des Sciences et Technologies de Lille, 59655 Villeneuve d'Ascq Cedex, France.
authors.forename: Jean-Pierre
authors.initials: JP
authors.lastname: Bohin
authors.affiliation: Unité de Glycobiologie Structurale et Fonctionnelle, UMR USTL-CNRS 8576 IFR 118, Université des Sciences et Technologies de Lille, 59655 Villeneuve d'Ascq Cedex, France.
authors.forename: Jean-Marie
authors.initials: JM
authors.lastname: Lacroix
mesh_terms: D001426:Bacterial Proteins / Q000032:analysis* / Q000302:isolation & purification; D016974:Dickeya chrysanthemi / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism / Q000472:pathogenicity; D015180:Electrophoresis, Gel, Two-Dimensional; D015964:Gene Expression Regulation, Bacterial; D005936:Glucans / Q000096:biosynthesis* / Q000235:genetics; D013058:Mass Spectrometry; D053858:Metabolic Networks and Pathways; D018832:Molecular Chaperones / Q000096:biosynthesis; D009154:Mutation; D010447:Peptide Hydrolases / Q000096:biosynthesis; D020543:Proteome / Q000032:analysis* / Q000302:isolation & purification; D040901:Proteomics; D014774:Virulence / Q000235:genetics
chemical_list: D001426:Bacterial Proteins; D005936:Glucans; D018832:Molecular Chaperones; D020543:Proteome; D010447:Peptide Hydrolases