title: Unraveling the effects of static magnetic field stress on cytosolic proteins of Salmonella by using a proteomic approach.
abstract: The present study investigated the adaptation of Salmonella enterica subsp. enterica serovar Hadar to static magnetic field (SMF) exposure (200 mT, 9 h). The proteomic analysis provides an overview of potentially important cytosolic proteins that Salmonella needs to regulate to survive and adapt to magnetic stress. Via 2-dimensional electrophoresis and liquid chromatography tandem mass spectrometry, we compared cytosolic proteomes before and after exposure to magnetic field. A total of 35 proteins displaying more than a 2-fold change were differentially expressed in exposed cells, among which 25 were upregulated and 10 were downregulated. These proteins can be classified mainly into 6 categories: (i) proteins involved in metabolic pathways of carbohydrates, (ii) chaperones and proteins produced in response to oxidative stress, (iii) proteins involved in energy homeostasis, (iv) elongation factors (EF-Tu and EF-Ts), (v) proteins involved in motility, and (vi) proteins involved in molecules transport. Many of the presented observations could be explained, while some represent still-unknown mechanisms. In addition, this study reveals 5 hypothetical proteins. It seems that the stress response to SMF (200 mT) is essentially set up to avoid oxidative damages, with the overexpression of proteins directly involved in oxidative stress response and metabolic switches to counteract oxidative stress. Interestingly, several proteins induced under SMF exposure are found to overlap with those induced by other stresses, such as heat shock and starvation.
authors.affiliation: a Laboratoire de Biochimie et Biologie Moléculaire, Faculté des Sciences de Bizerte, Université de Carthage, 7021 Zarzouna, Bizerte, Tunisie.|b UMR 6270 CNRS, Faculté des sciences, Université de Rouen, 76821 Mont Saint Aignan Cedex, France.
authors.forename: Sarra
authors.initials: S
authors.lastname: Snoussi
authors.affiliation: a Laboratoire de Biochimie et Biologie Moléculaire, Faculté des Sciences de Bizerte, Université de Carthage, 7021 Zarzouna, Bizerte, Tunisie.
authors.forename: Alya
authors.initials: A
authors.lastname: El May
authors.affiliation: b UMR 6270 CNRS, Faculté des sciences, Université de Rouen, 76821 Mont Saint Aignan Cedex, France.
authors.forename: Laurent
authors.initials: L
authors.lastname: Coquet
authors.affiliation: b UMR 6270 CNRS, Faculté des sciences, Université de Rouen, 76821 Mont Saint Aignan Cedex, France.
authors.forename: Philippe
authors.initials: P
authors.lastname: Chan
authors.affiliation: b UMR 6270 CNRS, Faculté des sciences, Université de Rouen, 76821 Mont Saint Aignan Cedex, France.
authors.forename: Thierry
authors.initials: T
authors.lastname: Jouenne
authors.affiliation: b UMR 6270 CNRS, Faculté des sciences, Université de Rouen, 76821 Mont Saint Aignan Cedex, France.
authors.forename: Emmanuelle
authors.initials: E
authors.lastname: Dé
authors.affiliation: a Laboratoire de Biochimie et Biologie Moléculaire, Faculté des Sciences de Bizerte, Université de Carthage, 7021 Zarzouna, Bizerte, Tunisie.
authors.forename: Ahmed
authors.initials: A
authors.lastname: Landoulsi
mesh_terms: D000222:Adaptation, Physiological; D001426:Bacterial Proteins / Q000378:metabolism*; D003600:Cytosol / Q000378:metabolism; D004734:Energy Metabolism; D015964:Gene Expression Regulation, Bacterial; D060526:Magnetic Fields; D053858:Metabolic Networks and Pathways; D018832:Molecular Chaperones / Q000378:metabolism; D010445:Peptide Elongation Factors / Q000378:metabolism; D020543:Proteome / Q000378:metabolism*; D040901:Proteomics; D019779:Salmonella enterica / Q000378:metabolism*
chemical_list: D001426:Bacterial Proteins; D018832:Molecular Chaperones; D010445:Peptide Elongation Factors; D020543:Proteome; C023512:elongation factor Ts
keywords: Salmonella; champ magnétique statique; cytosolic proteome; protéome cytosoliques; static magnetic field