The stress proteome of Enterococcus faecalis

• Published in: Electrophoresis Vol. 22; no. 14; pp. 2947 - 2954
• Main Authors: Giard, Jean-Christophe, Laplace, Jean-Marie, Rincé, Alain, Pichereau, Vianney, Benachour, Abdellah, Leboeuf, Céline, Flahaut, Sigrid, Auffray, Yanick, Hartke, Axel
• Format: Journal Article
• Language: English
• Published: Hoboken Wiley Subscription Services, Inc., A Wiley Company 01.08.2001; Wiley-VCH Verlag
• Subjects: Acids; Acids - pharmacology; Amino Acid Sequence; Bacterial Proteins; Bacterial Proteins - analysis; Bacterial Proteins - biosynthesis; Bacterial Proteins - classification; Bacterial Proteins - genetics; Bacteriology; Bile Acids and Salts; Bile Acids and Salts - pharmacology; Biochemistry, Molecular Biology; Blotting, Western; Cadmium Chloride; Cadmium Chloride - pharmacology; Databases, Protein; Detergents; Detergents - pharmacology; DNA-Binding Proteins; DNA-Binding Proteins - biosynthesis; DNA-Binding Proteins - genetics; DNA-Binding Proteins - physiology; Electrophoresis, Gel, Two-Dimensional; Enterococcus faecalis; Enterococcus faecalis - chemistry; Enterococcus faecalis - drug effects; Enterococcus faecalis - genetics; Enterococcus faecalis - physiology; Enzymes; Enzymes - analysis; Enzymes - biosynthesis; Enzymes - genetics; Gene Expression Regulation, Bacterial; Gene Expression Regulation, Bacterial - drug effects; Genomics; Glucose; Glucose - pharmacology; Hydrogen Peroxide; Hydrogen Peroxide - pharmacology; Life Sciences; Mercuric Chloride; Mercuric Chloride - pharmacology; Microbiology and Parasitology; Molecular Sequence Data; Open Reading Frames; Oxidative Stress; Proteome; Repressor Proteins; Repressor Proteins - biosynthesis; Repressor Proteins - genetics; Repressor Proteins - physiology; Sequence Homology, Amino Acid; Silver Staining; Sodium Dodecyl Sulfate; Sodium Dodecyl Sulfate - pharmacology; Starvation response; Stress response; Terminology as Topic; Cadmium Chloride; Enterococcus faecalis; Bacterial; Amino Acid; Oxidative Stress; Open Reading Frames; Repressor Proteins; Hydrogen Peroxide; Molecular Sequence Data; Glucose; Blotting; Western; Sequence Homology; Databases; Electrophoresis; DNA-Binding Proteins; Amino Acid Sequence; Enzymes; Silver Staining; Gene Expression Regulation; Terminology as Topic; Proteome; Detergents; Bile Acids and Salts; Sodium Dodecyl Sulfate; Protein; Bacterial Proteins; Gel; Two-Dimensional; Mercuric Chloride; Acids
• ISSN: 0173-0835; 1522-2683
• DOI: 10.1002/1522-2683(200108)22:14<2947::AID-ELPS2947>3.0.CO;2-K

Enterococcus faecalisis a resident bacterium of the intestinal tract of humans and animals. This bacterium can be responsible for serious diseases and is one of the largest causes of hospital‐based infections. This hardy organism resists many kinds of stresses and is used as a major indicator of the hygienic quality of food, milk, and drinking water. On the other side, enterococci seem to have beneficial role in the development of cheese aroma and are added in certain starter cultures. Since ten years, our laboratory has used the two‐dimensional electrophoresis (2‐DE) technique to study the response of E. faecalis to physical or chemical stresses as well as to glucose and total starvation. Twenty‐seven protein spots on 2‐D gels have been identified by N‐terminal sequencing or Western blotting which make up the first proteome database of this species. The proteins were classified in four different groups according to their function and their regulation. The first group comprises well‐characterized proteins with known protective functions towards stresses. The second group contains enzymes of catabolic pathways. Their implication in stress resistance seems not obvious. A third group are proteins induced in glucose‐starved cells belonging to the CcpA regulon. Induction of these enzymes under starvation may serve to increase the scavenging capacity of the cells for nutrients or may be important to mobilize endogenous energetic reserves. Lastly, nine N‐terminal amino acid sequences or open reading frames (ORF) showed no homologies with sequences in databases. A comprehensive description of stress proteins of E. faecalisand analysis of their patterns of expression under different environmental conditions would greatly increase our understanding of the molecular mechanisms underlying the extraordinary capacity of this bacterium to survive under hostile conditions.