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Identification of secreted and surface proteins from Enterococcus faecalis
Abdellah Benachour1, Thierry Morin, Laurent Hébert
1USC INRA, IFR, Universite de Caen, France. abdellah.benachour@unicaen.fr
Canadian Journal of Microbiology
|November 10, 2009
Summary
This study identified 44 secreted and surface proteins in Enterococcus faecalis, a common cause of hospital infections. These findings advance understanding of bacterial virulence factors and potential therapeutic targets.
Area of Science:
- Microbiology
- Proteomics
- Bacterial Pathogenesis
Background:
- Secreted and surface proteins are crucial for bacterial interaction with the environment.
- Enterococcus faecalis is a major cause of nosocomial infections, with some proteins identified as virulence factors.
Purpose of the Study:
- To identify abundant secreted and surface-associated proteins of the Enterococcus faecalis JH2-2 strain using a global proteomic approach.
- To characterize these proteins for potential roles in virulence and as therapeutic targets.
Main Methods:
- Global proteomic analysis of Enterococcus faecalis JH2-2.
- Separation of proteins via gel electrophoresis and in vivo trypsinolysis.
- Analysis using liquid chromatography-electrospray ionization ion trap tandem mass spectrometry.
Main Results:
- Identified a total of 44 proteins: 8 secreted and 38 cell surface proteins.
- 35 of the 44 identified proteins possess signal peptides or transmembrane domains, indicating extracellular localization.
- Two proteins were common to both secreted and cell surface groups.
Conclusions:
- This proteomic study provides a comprehensive list of E. faecalis secreted and surface proteins.
- The findings support further proteomic investigations into E. faecalis surface proteins for virulence factor discovery.
- This research may contribute to the development of novel therapeutic strategies against enterococcal infections.
