• DOI:10.1099/MIC.0.27534-0
• Corpus ID: 13929465

Identification and preliminary characterization of cell-wall-anchored proteins of Staphylococcus epidermidis.

@article{Bowden2005IdentificationAP,
  title={Identification and preliminary characterization of cell-wall-anchored proteins of Staphylococcus epidermidis.},
  author={Maria Gabriela Bowden and Wei Chen and Jenny Singvall and Yi Xu and Sharon J. Peacock and Viviana Valtulina and Pietro Speziale and Magnus Höök},
  journal={Microbiology},
  year={2005},
  volume={151 Pt 5},
  pages={
          1453-64
        }
}

• M. Bowden, Wei Chen, +5 authors M. Höök
• Published 1 May 2005
• Biology
• Microbiology

Staphylococcus epidermidis is a ubiquitous human skin commensal that has emerged as a major cause of foreign-body infections. Eleven genes encoding putative cell-wall-anchored proteins were identified by computer analysis of the publicly available S. epidermidis unfinished genomic sequence. Four genes encode previously described proteins (Aap, Bhp, SdrF and SdrG), while the remaining seven have not been characterized. Analysis of primary sequences of the Staphylococcus epidermidis surface (Ses) proteins indicates that they have a structural organization similar to the previously described cell-wall-anchored proteins from S. aureus and other Gram-positive cocci. However, not all of the Ses proteins are direct homologues of the S. aureus proteins. Secondary and tertiary structure predictions suggest that most of the Ses proteins are composed of several contiguous subdomains, and that the majority of these predicted subdomains are folded into beta-rich structures. PCR analysis indicates that certain genes may be found more frequently in disease isolates compared to strains isolated from healthy skin. Patients recovering from S. epidermidis infections had higher antibody titres against some Ses proteins, implying that these proteins are expressed during human infection. Western blot analyses of early-logarithmic and late-stationary in vitro cultures suggest that different regulatory mechanisms control the expression of the Ses proteins.