@article{MakgotlhoMarincolaSchaeferetal.2013,
  author    = {Makgotlho, Phuti E. and Marincola, Gabriella and Sch{\"a}fer, Daniel and Liu, Quian and Bae, Taeok and Geiger, Tobias and Wasserman, Elizabeth and Wolz, Christine and Ziebuhr, Wilma and Sinha, Bhanu},
  title     = {SDS Interferes with SaeS Signaling of Staphylococcus aureus Independently of SaePQ},
  series = {PLOS ONE},
  volume    = {8},
  journal   = {PLOS ONE},
  number    = {8},
  issn      = {1932-6203},
  doi       = {10.1371/journal.pone.0071644},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-128469},
  pages     = {e71644},
  year      = {2013},
  abstract  = {The Staphylococcus aureus regulatory saePQRS system controls the expression of numerous virulence factors, including extracellular adherence protein (Eap), which amongst others facilitates invasion of host cells. The saePQRS operon codes for 4 proteins: the histidine kinase SaeS, the response regulator SaeR, the lipoprotein SaeP and the transmembrane protein SaeQ. S. aureus strain Newman has a single amino acid substitution in the transmembrane domain of SaeS (L18P) which results in constitutive kinase activity. SDS was shown to be one of the signals interfering with SaeS activity leading to inhibition of the sae target gene eap in strains with SaeS(L) but causing activation in strains containing SaeS(P). Here, we analyzed the possible involvement of the SaeP protein and saePQ region in SDS-mediated sae/eap expression. We found that SaePQ is not needed for SDS-mediated SaeS signaling. Furthermore, we could show that SaeS activity is closely linked to the expression of Eap and the capacity to invade host cells in a number of clinical isolates. This suggests that SaeS activity might be directly modulated by structurally non-complex environmental signals, as SDS, which possibly altering its kinase/phosphatase activity.},
  language  = {en}
}