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Open Access Highly Accessed Research article

Identification of surface proteins in Enterococcus faecalis V583

Liv Anette Bøhle1, Tahira Riaz1, Wolfgang Egge-Jacobsen2, Morten Skaugen1, Øyvind L Busk1, Vincent GH Eijsink1 and Geir Mathiesen1*

Author affiliations

1 Department of Chemistry, Biotechnology, and Food Science, The Norwegian University of Life Sciences, 1432 Ås, Norway

2 Department of Molecular Biosciences, Glyconor Mass Spectrometry, University of Oslo, 0316 Oslo, Norway

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Citation and License

BMC Genomics 2011, 12:135  doi:10.1186/1471-2164-12-135

Published: 1 March 2011

Abstract

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.