Open AccessThe role of ionic interactions in the adherence of the S taphylococcus epidermidis adhesin SdrF to prosthetic material
Author(s) -
Toba Faustino A.,
Visai Livia,
Trivedi Sheetal,
Lowy Franklin D.
Publication year - 2013
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/1574-6968.12018
Subject(s) - bacterial adhesin , staphylococcus epidermidis , microbiology and biotechnology , ionic bonding , staphylococcus , chemistry , staphylococcus aureus , escherichia coli , biology , bacteria , biochemistry , genetics , ion , organic chemistry , gene
S taphylococcus epidermidis infections are common complications of prosthetic device implantation. SdrF, a surface protein, appears to play a critical role in the initial colonization step by adhering to type I collagen and Dacron™. The role of ionic interactions in S . epidermidis adherence to prosthetic material was examined. SdrF was cloned and expressed in L actococcus lactis . The effect of pH, cation concentration, and detergents on adherence to different types of plastic surfaces was assessed by crystal violet staining and bacterial cell counting. SdrF, in contrast with controls and other S . epidermidis surface proteins, bound to hydrophobic materials such as polystyrene. Binding was an ionic interaction and was affected by surface charge of the plastic, pH, and cation concentration. Adherence of the SdrF construct was increased to positively charged plastics and was reduced by increasing concentrations of Ca 2+ and Na + . Binding was optimal at pH 7.4. Kinetic studies demonstrated that the SdrF B domain as well as one of the B subdomains was sufficient to mediate binding. The SdrF construct also bound more avidly to Goretex™ than the lacotococcal control. SdrF is a multifunctional protein that contributes to prosthetic devices infections by ionic, as well as specific receptor–ligand interactions.