TY  - JOUR
A1  - Neumann, Yvonne
A1  - Ohlsen, Knut
A1  - Donat, Stefanie
A1  - Engelmann, Susanne
A1  - Kusch, Harald
A1  - Albrecht, Dirk
A1  - Cartron, Michael
A1  - Hurd, Alexander
A1  - Foster, Simon J.
T1  - The effect of skin fatty acids on Staphylococcus aureus
JF  - Archives of Microbiology
N2  - Staphylococcus aureus is a commensal of the human nose and skin. Human skin fatty acids, in particular cis-6-hexadecenoic acid (C-6-H), have high antistaphylococcal activity and can inhibit virulence determinant production. Here, we show that sub-MIC levels of C-6-H result in induction of increased resistance. The mechanism(s) of C-6-H activity was investigated by combined transcriptome and proteome analyses. Proteome analysis demonstrated a pleiotropic effect of C-6-H on virulence determinant production. In response to C-6-H, transcriptomics revealed altered expression of over 500 genes, involved in many aspects of virulence and cellular physiology. The expression of toxins (hla, hlb, hlgBC) was reduced, whereas that of host defence evasion components (cap, sspAB, katA) was increased. In particular, members of the SaeRS regulon had highly reduced expression, and the use of specific mutants revealed that the effect on toxin production is likely mediated via SaeRS
KW  - S. aureus
KW  - skin fatty acid
KW  - C-6-H
KW  - resistance
Y1  - 2015
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-121657
VL  - 197
ER  - 
TY  - JOUR
A1  - Rakette, Sonja
A1  - Donat, Stefanie
A1  - Ohlsen, Knut
A1  - Stehle, Thilo
T1  - Structural Analysis of Staphylococcus aureus Serine/Threonine Kinase PknB
JF  - PLoS One
N2  - Effective treatment of infections caused by the bacterium Staphylococcus aureus remains a worldwide challenge, in part due to the constant emergence of new strains that are resistant to antibiotics. The serine/threonine kinase PknB is of particular relevance to the life cycle of S. aureus as it is involved in the regulation of purine biosynthesis, autolysis, and other central metabolic processes of the bacterium. We have determined the crystal structure of the kinase domain of PknB in complex with a non-hydrolyzable analog of the substrate ATP at 3.0 angstrom resolution. Although the purified PknB kinase is active in solution, it crystallized in an inactive, autoinhibited state. Comparison with other bacterial kinases provides insights into the determinants of catalysis, interactions of PknB with ligands, and the pathway of activation.
KW  - SER/THR kinase
KW  - domain
KW  - subunit
KW  - dependent protein-kinase
KW  - mycobacterium-tuberculosis
KW  - activation mechanism
KW  - crystal structure
KW  - antibiotic resistance
KW  - catalytic
KW  - methicillin
KW  - inhibitor
Y1  - 2012
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-135369
VL  - 7
IS  - 6
ER  -