Affordable Access

deepdyve-link deepdyve-link
Publisher Website

Identification of secreted and surface proteins from Enterococcus faecalis.

Authors
  • Benachour, Abdellah
  • Morin, Thierry
  • Hébert, Laurent
  • Budin-Verneuil, Aurélie
  • Le Jeune, André
  • Auffray, Yanick
  • Pichereau, Vianney
Type
Published Article
Journal
Canadian Journal of Microbiology
Publisher
Canadian Science Publishing
Publication Date
Aug 01, 2009
Volume
55
Issue
8
Pages
967–974
Identifiers
DOI: 10.1139/w09-052
PMID: 19898536
Source
Medline
License
Unknown

Abstract

Secreted and surface proteins of bacteria are key molecules that interface the cell with the environment. Some of them, corresponding to virulence factors, have already been described for Enterococcus faecalis, the predominant species involved in enterococcal nosocomial infections. In a global proteomic approach, the identification of the most abundant secreted and surface-associated proteins of E. faecalis JH2-2 strain was carried out. These proteins were separated by gel electrophoresis or directly subjected to in vivo trypsinolysis and then analyzed by liquid chromatography - electrospray ion trap tandem mass spectrometry. Putative functions were assigned by homology to the translated genomic database of E. faecalis. A total of 44 proteins were identified, eight secreted proteins from the supernatant culture and 38 cell surface proteins from two-dimensional gel electrophoresis and in vivo trypsinolysis among which two are common to the two groups. Their sequences analysis revealed that 35 of the 44 proteins harbour characteristic features (signal peptide or transmembrane domains) consistent with an extracellular localization. This study may be considered as an important step to encourage proteomic-based investigations of E. faecalis cell surface associated proteins that could lead to the discovery of virulence factors and to the development of new therapeutic tools.

Report this publication

Statistics

Seen <100 times