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dc.contributor.authorBøhle, Liv A
dc.contributor.authorRiaz, Tahira
dc.contributor.authorEgge-Jacobsen, Wolfgang
dc.contributor.authorSkaugen, Morten
dc.contributor.authorBusk, Øyvind L
dc.contributor.authorEijsink, Vincent G
dc.contributor.authorMathiesen, Geir
dc.date.accessioned2015-10-09T01:14:07Z
dc.date.available2015-10-09T01:14:07Z
dc.date.issued2011
dc.identifier.citationBMC Genomics. 2011 Mar 01;12(1):135
dc.identifier.urihttp://hdl.handle.net/10852/46455
dc.description.abstractBackground 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.
dc.language.isoeng
dc.rightsBøhle et al; licensee BioMed Central Ltd.
dc.rightsAttribution 2.0 Generic
dc.rights.urihttp://creativecommons.org/licenses/by/2.0/
dc.titleIdentification of surface proteins in Enterococcus faecalis V583
dc.typeJournal article
dc.date.updated2015-10-09T01:14:08Z
dc.creator.authorBøhle, Liv A
dc.creator.authorRiaz, Tahira
dc.creator.authorEgge-Jacobsen, Wolfgang
dc.creator.authorSkaugen, Morten
dc.creator.authorBusk, Øyvind L
dc.creator.authorEijsink, Vincent G
dc.creator.authorMathiesen, Geir
dc.identifier.doihttp://dx.doi.org/10.1186/1471-2164-12-135
dc.identifier.urnURN:NBN:no-50604
dc.type.documentTidsskriftartikkel
dc.type.peerreviewedPeer reviewed
dc.identifier.fulltextFulltext https://www.duo.uio.no/bitstream/handle/10852/46455/1/12864_2010_Article_3270.pdf
dc.type.versionPublishedVersion
cristin.articleid135


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