A proteomic study of Escherichia coli O157:H7 NCTC 12900 cultivated in biofilm or in planktonic growth mode.
Escherichia coli 0157:H7 biofilms were studied by a new method of cultivation in order to identify some of the proteins involved in the biofilm phenotype. A proteomic analysis of sessile or planktonic bacteria of the same age was carried out by two-dimensional electrophoresis, matrix-assisted laser desorption ionization-time of flight mass spectrometry (MALDI-TOF-MS) and database searching. Comparison of two-dimensional gels showed clear differences between protein patterns of sessile and planktonic cells. Fourteen proteins increased in biofilms, whereas three decreased. From these 17 proteins, 10 were identified by MALDI-TOF-MS and could be classified into four categories according to their function: (1) general metabolism proteins (malate dehydrogenase, thiamine-phosphate pyrophosphorylase), (2) sugar and amino acid transporters (D-ribose-binding periplasmic protein, D-galactose-binding protein, YBEJ), (3) regulator proteins (DNA starvation protein and H-NS) and (4) three proteins with unknown function. The results of this study showed that E. coli O157:H7 modified the expression of several proteins involved in biofilm growth mode.
Trémoulet
Frédéric
F
Station de Recherches sur la Viande, Laboratoire de Microbiologie, Institut National de la Recherche Agronomique, Theix, 63122, Saint Genès Champanelle, France.
Duché
Ophélie
O
Namane
Abdelkader
A
Martinie
Brigitte
B
Labadie
Jean-Claude
JC
D000595:Amino Acid Sequence; D018441:Biofilms / Q000254:growth & development*; D015180:Electrophoresis, Gel, Two-Dimensional; D019453:Escherichia coli O157 / Q000737:chemistry* / Q000254:growth & development* / Q000648:ultrastructure; D029968:Escherichia coli Proteins / Q000032:analysis* / Q000737:chemistry; D008855:Microscopy, Electron, Scanning; D008969:Molecular Sequence Data; D040901:Proteomics; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
D029968:Escherichia coli Proteins