The stress proteome of Enterococcus faecalis.
Enterococcus faecalis is 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. faecalis and 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.
Giard
J C
JC
Laboratoire de Microbiologie de l'Environnement, Université de Caen, France. giard@ibba.unicaen.fr
Laplace
J M
JM
Rincé
A
A
Pichereau
V
V
Benachour
A
A
Leboeuf
C
C
Flahaut
S
S
Auffray
Y
Y
Hartke
A
A
D000143:Acids / Q000494:pharmacology; D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000032:analysis* / Q000096:biosynthesis / Q000145:classification / Q000235:genetics; D001647:Bile Acids and Salts / Q000494:pharmacology; D015153:Blotting, Western; D019256:Cadmium Chloride / Q000494:pharmacology; D004268:DNA-Binding Proteins / Q000096:biosynthesis / Q000235:genetics / Q000502:physiology; D030562:Databases, Protein; D003902:Detergents / Q000494:pharmacology; D015180:Electrophoresis, Gel, Two-Dimensional; D013293:Enterococcus faecalis / Q000737:chemistry* / Q000187:drug effects / Q000235:genetics / Q000502:physiology; D004798:Enzymes / Q000032:analysis / Q000096:biosynthesis / Q000235:genetics; D015964:Gene Expression Regulation, Bacterial / Q000187:drug effects; D005947:Glucose / Q000494:pharmacology; D006861:Hydrogen Peroxide / Q000494:pharmacology; D008627:Mercuric Chloride / Q000494:pharmacology; D008969:Molecular Sequence Data; D016366:Open Reading Frames; D018384:Oxidative Stress; D020543:Proteome; D012097:Repressor Proteins / Q000096:biosynthesis / Q000235:genetics / Q000502:physiology; D017386:Sequence Homology, Amino Acid; D016622:Silver Staining; D012967:Sodium Dodecyl Sulfate / Q000494:pharmacology; D009626:Terminology as Topic
D000143:Acids; D001426:Bacterial Proteins; D001647:Bile Acids and Salts; D004268:DNA-Binding Proteins; D003902:Detergents; D004798:Enzymes; D020543:Proteome; D012097:Repressor Proteins; C069286:catabolite control proteins, bacteria; D012967:Sodium Dodecyl Sulfate; D008627:Mercuric Chloride; D006861:Hydrogen Peroxide; D005947:Glucose; D019256:Cadmium Chloride