Abstract
Triton X-100 (TX-100), a useful non-ionic surfactant, reduced the methicillin resistance in Staphylococcus aureus significantly. Many S. aureus proteins were expressed in the presence of TX-100. SarA, one of the TX-100-induced proteins, acts as a global virulence regulator in S. aureus. To understand the effects of TX-100 on the structure, and function of SarA, a recombinant S. aureus SarA (rSarA) and its derivative (C9W) have been investigated in the presence of varying concentrations of this surfactant using various probes. Our data have revealed that both rSarA and C9W bind to the cognate DNA with nearly similar affinity in the absence of TX-100. Interestingly, their DNA binding activities have been significantly increased in the presence of pre-micellar concentration of TX-100. The increase of TX-100 concentrations to micellar or post-micellar concentration did not greatly enhance their activities further. TX-100 molecules have altered the secondary and tertiary structures of both proteins to some extents. Size of the rSarA-TX-100 complex appears to be intermediate to those of rSarA and TX-100. Additional analyses show a relatively moderate interaction between C9W and TX-100. Binding of TX-100 to C9W has, however, occurred by a cooperative pathway particularly at micellar and higher concentrations of this surfactant. Taken together, TX-100-induced structural alteration of rSarA and C9W might be responsible for their increased DNA binding activity. As TX-100 has stabilized the somewhat weaker SarA-DNA complex effectively, it could be used to study its structure in the future.
Highlights
Staphylococcus aureus, a Gram-positive bacterium, encodes various virulence factors and virulence regulators for causingPLOS ONE | DOI:10.1371/journal.pone.0151426 March 18, 2016Effects of Triton X-100 on SarA study design, data collection and analysis, decision to publish, or preparation of the manuscript
We have investigated the effects of Triton X-100 (TX-100) on the structure and function of a recombinant SarA and its mutant (C9W) by various in vitro methods
Our data have demonstrated a significant increase of the DNA binding activity of both recombinant S. aureus SarA (rSarA) and C9W in the presence of pre-micellar, micellar, and post-micellar concentrations of TX-100
Summary
Staphylococcus aureus, a Gram-positive bacterium, encodes various virulence factors (such as enterotoxins, α-hemolysin, exfoliative toxins, protein A, β-hemolysin, clumping factor, δhemolysin, fibronectin-binding protein, phenol-soluble modulins, iron-uptake protein, proteases, capsule, lipases, biofilm, nucleases, Panton-Valentine leukocidin, peptidoglycan hydrolases, etc.) and virulence regulators (namely, agr, sarA, saeRS, codY, sigB, etc.) for causingPLOS ONE | DOI:10.1371/journal.pone.0151426 March 18, 2016Effects of Triton X-100 on SarA study design, data collection and analysis, decision to publish, or preparation of the manuscript. Staphylococcus aureus, a Gram-positive bacterium, encodes various virulence factors (such as enterotoxins, α-hemolysin, exfoliative toxins, protein A, β-hemolysin, clumping factor, δhemolysin, fibronectin-binding protein, phenol-soluble modulins, iron-uptake protein, proteases, capsule, lipases, biofilm, nucleases, Panton-Valentine leukocidin, peptidoglycan hydrolases, etc.) and virulence regulators (namely, agr, sarA, saeRS, codY, sigB, etc.) for causing. Effects of Triton X-100 on SarA study design, data collection and analysis, decision to publish, or preparation of the manuscript
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