Identification of surface proteins in XXXX .

@entity1 @entity8516 @entity26 @entity22178 @entity797 @entity5681 @entity597
BACKGROUND: Surface proteins are a key to a deeper understanding of the behaviour of Gram-positive bacteria interacting with the @entity1 gastro-intestinal tract. Such proteins contribute to cell wall synthesis and maintenance and are important for interactions between the bacterial cell and the @entity1 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 @entity22178 . 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 @entity597 groups in mucin and a lipid-anchored @entity8516 reductase that could contribute to generation of reactive @entity26 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, @entity5681 -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 @entity797 and its environment.
