A proteomic study of Escherichia coli O157:H7 NCTC 12900 cultivated in biofilm or in planktonic growth mode
Autor: | Jean-Claude Labadie, Frédéric Trémoulet, Brigitte Martinie, Ophélie Duché, Abdelkader Namane |
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Rok vydání: | 2002 |
Předmět: |
Proteomics
Molecular Sequence Data Biology medicine.disease_cause Escherichia coli O157 Microbiology Malate dehydrogenase Genetics medicine Electrophoresis Gel Two-Dimensional Amino Acid Sequence Molecular Biology Escherichia coli chemistry.chemical_classification Escherichia coli Proteins Biofilm Periplasmic space biology.organism_classification Enterobacteriaceae Amino acid chemistry Biofilms Spectrometry Mass Matrix-Assisted Laser Desorption-Ionization Proteome Microscopy Electron Scanning Bacteria |
Zdroj: | FEMS microbiology letters. 215(1) |
ISSN: | 0378-1097 |
Popis: | 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. |
Databáze: | OpenAIRE |
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