Salt stress proteins induced in Listeria monocytogenes.
The ability of Listeria monocytogenes to tolerate salt stress is of particular importance, as this pathogen is often exposed to such environments during both food processing and food preservation. In order to understand the survival mechanisms of L. monocytogenes, an initial approach using two-dimensional polyacrylamide gel electrophoresis was performed to analyze the pattern of protein synthesis in response to salt stress. Of 400 to 500 visible proteins, the synthesis of 40 proteins (P < 0.05) was repressed or induced at a higher rate during salt stress. Some of the proteins were identified on the basis of mass spectrometry or N-terminal sequence analysis and database searching. Twelve proteins showing high induction after salt stress were similar to general stress proteins (Ctc and DnaK), transporters (GbuA and mannose-specific phosphotransferase system enzyme IIAB), and general metabolism proteins (alanine dehydrogenase, CcpA, CysK, EF-Tu, Gap, GuaB, PdhA, and PdhD).
Duché
Ophélie
O
Station de Recherches sur la Viande, Institut National de la Recherche Agronomique, Theix, 63122 Saint-Genès Champanelle, France.
Trémoulet
Frédéric
F
Glaser
Philippe
P
Labadie
Jean
J
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism; D015180:Electrophoresis, Gel, Two-Dimensional; D006360:Heat-Shock Proteins / Q000737:chemistry / Q000378:metabolism*; D018869:Heat-Shock Response; D008089:Listeria monocytogenes / Q000254:growth & development / Q000502:physiology*; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D010449:Peptide Mapping; D012965:Sodium Chloride / Q000494:pharmacology*
D001426:Bacterial Proteins; D006360:Heat-Shock Proteins; D012965:Sodium Chloride