A proteomic analysis of the salt stress response of Listeria monocytogenes.
Protein variations in Listeria monocytogenes were analyzed by 2-D electrophoresis. Bacteria were grown either in a rich medium or in a chemically defined medium. Three proteins, which are more expressed in the chemically defined medium than in the rich medium, were identified by mass spectrometry. They are closely related to AppA, Ctc and YvyD. After an osmotic shock, according to the medium and the NaCl concentration, the synthesis rate (P<0.05) of 59 proteins is altered by salinity. Half of them were more expressed, some of these proteins were closely related to Ctc, GbuA and the 30S ribosomal protein S6. Among the proteins which were down-expressed in the presence of salt, two were similar to AckA and PdhD.
Duché
Ophélie
O
Station de Recherches sur la Viande, Institut National de la Recherche Agronomique, 63122, Saint-Genès Champanelle, France.
Trémoulet
Frédéric
F
Namane
Abdelkader
A
Labadie
Jean
J
D001426:Bacterial Proteins / Q000378:metabolism*; D003470:Culture Media; D015180:Electrophoresis, Gel, Two-Dimensional; D006360:Heat-Shock Proteins / Q000378:metabolism*; D018869:Heat-Shock Response; D006801:Humans; D008089:Listeria monocytogenes / Q000187:drug effects* / Q000378:metabolism / Q000502:physiology; D013058:Mass Spectrometry; D020543:Proteome; D012965:Sodium Chloride / Q000494:pharmacology*
D001426:Bacterial Proteins; D003470:Culture Media; D006360:Heat-Shock Proteins; D020543:Proteome; D012965:Sodium Chloride