The recently published Enterococcus faecalis genome [Paulsen, I. T., Banerjei, L., Myers, G. S. & 29 other authors (2003). Science 299, 2071-2074)] was examined and 41 putative cell-wall-anchored
proteins were identified. Seventeen of these
proteins are predicted to contain tandemly repeated
immunoglobulin-like folds characteristic of the structural organization of staphylococcal adhesins of the MSCRAMM (microbial surface component recognizing adhesive matrix molecules) type. Two of the nine
proteins selected for further study appear to represent cell-wall-anchored
enzymes. It is proposed that the remaining seven
proteins constitute a family of structurally related
proteins potentially interacting with
proteins of the host. This family includes the previously identified
collagen/
laminin-binding MSCRAMM ACE [Rich, R. L., Kreikemeyer, B., Owens, R. T., LaBrenz, S., Narayana, S. V., Weinstock, G. M., Murray, B. E. & Hook, M. (1999). J Biol Chem 274, 26939-26945]. It is further demonstrated that genes encoding the seven putative MSCRAMMs are present in all E. faecalis strains tested and these
proteins appear to be expressed during
infection in humans, since sera from infected individuals contain
antibodies reacting with recombinant versions of the enterococcal
proteins.