Identification of secreted and surface proteins from Enterococcus faecalis
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.
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Extracellular DnaK, enolase, and GAPDH were identified in this study and in E. faecalis JH2-2; these proteins may play an important role in bacterial adhesion.
“Extracellular DnaK, enolase, and GAPDH were identified in this study and in the laboratory strain, E. faecalis JH2-2 (Benachour et al., 2009), these proteins may play an important role in bacterial adhesion, as they have been reported to have a strong binding capacity to human thrombospondin (Schaumburg et al., 2004).”
From Adhesion and Colonization of the Probiotic Lactobacillus plantarum HC-2 in the Intestine of Litopenaeus Vannamei Are Associated With Bacterial Surface Proteins (2022) · cites this paper as Benachour et al., 2009
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Identification of surface proteins in Enterococcus faecalis V583
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- Authors
- Benachour, A., Morin, T., Hébert, L., Budin-Verneuil, A., Le Jeune, A., Auffray, Y., & Pichereau, V.
- Affiliations
- Institut National de la Recherche Agronomique (FR)
- Laboratoire de Microbiologie de l’Environnement EA956, USC INRA 2017, IFR 146, Université de Caen, 14032 Caen cedex, France.
- Venue
- Canadian Journal of Microbiology
- Publisher
- Canadian Science Publishing
- Published
- 2009-08
- Volume
- 55
- Issue
- 8
- Pages
- 967-974
- ISSN
- 0008-4166 (ISSN-L)
- 1480-3275
- OpenAlex
- W2131649769
- Cited by
- 28
- References
- 28
- Citations by year
- 2023: 1 · 2022: 3 · 2020: 1 · 2019: 1 · 2018: 1 · 2017: 2 · 2016: 2 · 2015: 4 · 2014: 5 · 2013: 2 · 2012: 1
- FWCI
- 0.86
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Canadian Journal of Microbiology (publishedVersion)
- PubMed (publishedVersion)
- HAL (submittedVersion)
- Topics
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
- Keywords
- Enterococcus faecalis, secreted proteins, cell surface proteins, virulence factors, extracellular proteins, signal peptide, transmembrane domain, proteomics
- MeSH terms
- Bacterial Proteins, Membrane Proteins, Enterococcus faecalis, Proteomics
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