Identification of surface proteins in Enterococcus faecalis V583
Open accessAbstract
BACKGROUND: Surface proteins are a key to a deeper understanding of the behaviour of Gram-positive bacteria interacting with the human gastro-intestinal tract. Such proteins contribute to cell wall synthesis and maintenance and are important for interactions between the bacterial cell and the human host. Since they are exposed and may play roles in pathogenicity, surface proteins are interesting targets for drug design. RESULTS: Using methods based on proteolytic "shaving" of bacterial cells and subsequent mass spectrometry-based protein identification, we have identified surface-located proteins in Enterococcus faecalis V583. In total 69 unique proteins were identified, few of which have been identified and characterized previously. 33 of these proteins are predicted to be cytoplasmic, whereas the other 36 are predicted to have surface locations (31) or to be secreted (5). Lipid-anchored proteins were the most dominant among the identified surface proteins. The seemingly most abundant surface proteins included a membrane protein with a potentially shedded extracellular sulfatase domain that could act on the sulfate groups in mucin and a lipid-anchored fumarate reductase that could contribute to generation of reactive oxygen species. CONCLUSIONS: The present proteome analysis gives an experimental impression of the protein landscape on the cell surface of the pathogenic bacterium E. faecalis. The 36 identified secreted (5) and surface (31) proteins included several proteins involved in cell wall synthesis, pheromone-regulated processes, and transport of solutes, as well as proteins with unknown function. These proteins stand out as interesting targets for further investigation of the interaction between E. faecalis and its environment.
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EF-G, EF-P, and EF-Ts proteins were identified, implying an exposed localization similar to reports in E. faecalis V583 and B. subtilis.
“Except for EF-Tu, we also identified EF-G, EF-P, and EF-Ts proteins and this implies an exposed localization, similar to the report in E. faecalis V583 (Bøhle et al., 2011) and model B. subtilis (Tjalsma et al., 2008).”
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 Bøhle et al., 2011
The Protein identification table lists EF-G (elongation factor G) among proteins identified in E. faecalis V583, but labels its predicted localization cytoplasmic; it does not list EF-P or EF-Ts. In Results and discussion > Cytoplasmic proteins, the inference of exposed localization and comparison with B. subtilis concern ribosomal protein L7/L12, not these elongation factors. (LLM, conf=0.86)
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- Authors
- Bøhle, L. A., Riaz, T., Egge-Jacobsen, W., Skaugen, M., Busk, Ø. L., Eijsink, V. G., & Mathiesen, G.
- Affiliations
- Norwegian University of Life Sciences (NO)
- University of Oslo (NO)
- Corresponding author
- Mathiesen, Geir
- Venue
- BMC Genomics
- Published
- 2011-03-01
- Volume
- 12
- Issue
- 1
- Pages
- 135-135
- ISSN
- 1471-2164 (ISSN-L)
- PMC
- PMC3059304
- OpenAlex
- W1993183798
- Cited by
- 67
- References
- 68
- Citations by year
- 2025: 1 · 2024: 1 · 2023: 4 · 2022: 2 · 2021: 3 · 2020: 4 · 2019: 5 · 2018: 2 · 2017: 6 · 2016: 8 · 2015: 10 · 2014: 6 · 2013: 6 · 2012: 7
- FWCI
- 3.04
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- BMC Genomics (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- NORA - Norwegian Open Research Archives (submittedVersion, cc-by)
- Funders
- Norges Forskningsråd (183627, 183637)
- 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, surface proteins, cell surface proteome, lipid-anchored proteins, fumarate reductase, cell wall biosynthesis, bacterial pathogenicity, host-pathogen interaction, gastrointestinal tract, therapeutic target
- MeSH terms
- Amino Acid Sequence, Bacterial Proteins, Chromatography, Liquid, Electrophoresis, Polyacrylamide Gel, Membrane Proteins, Molecular Sequence Data, Enterococcus faecalis, Genome, Bacterial, Computational Biology, Proteome, Tandem Mass Spectrometry
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