The "landscape" of
biologically active substances present on the surface of Enterococcus faecalis V583 (E faecalis) has been studied using mass chromatography.
Scientists writing in BMC Genomics explain how they applied proteolytic shaving to the bacterial cells, following this by using mass spectrometry to identify the proteins present.
These biologically active substances were then examined to determine which were lipid-anchored, secreted, surface-located or cytoplasmic.
"Lipid-anchored proteins were the most dominant among the identified surface proteins," the scientists write.
Meanwhile, of the 69 unique proteins found, five were secreted, 31 surface-located and 33 cytoplasmic.
The surface and secreted proteins are particularly interesting, say the researchers, as possible avenues for future studies of E faecalis and the way in which it interacts with its surroundings.
BMC Genomics carries findings which relate to elements of both structural and functional proteomics and genomics.
In this study, the scientists involved were from the Norwegian University of Life Sciences and the University of Oslo.
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