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Figure 6 shows the impact of mutations in individual protease genes/operons on biofilm formation in vitro. The relative capacity to form a biofilm was assessed using a microtiter plate assay as previously described (Beenken et al. 2003) using FPR3757, its sarA mutant, and its sarA mutant carrying mutations in the indicated protease genes. Single asterisks indicate significance by comparison to the parent strain. Double asterisks indicate significance by comparison to the sarA mutant. As a control, biofilm formation was also assessed in LAC, its sarA mutant, and derivatives of thesarA mutant unable to produce aureolysin (Saur), unable to produce any extracellular protease (SP), or unable to produce any extracellular protease other than those encoded by the spl operon (SPspl+). Single asterisk indicates statistical significance by comparison to the sarA mutant. Double asterisks indicate significance by comparison to the Saur mutant.

Figure 6 shows the impact of mutations in individual protease genes/operons on biofilm formation in vitro. The relative capacity to form a biofilm was assessed using a microtiter plate assay as previously described (Beenken et al. 2003) using FPR3757, its sarA mutant, and its sarA mutant carrying mutations in the indicated protease genes. Single asterisks indicate significance by comparison to the parent strain. Double asterisks indicate significance by comparison to the sarA mutant. As a control, biofilm formation was also assessed in LAC, its sarA mutant, and derivatives of thesarA mutant unable to produce aureolysin (Saur), unable to produce any extracellular protease (SP), or unable to produce any extracellular protease other than those encoded by the spl operon (SPspl+). Single asterisk indicates statistical significance by comparison to the sarA mutant. Double asterisks indicate significance by comparison to the Saur mutant.

Figure 6 shows the impact of mutations in individual protease genes/operons on biofilm formation in vitro. The relative capacity to form a biofilm was assessed using a microtiter plate assay as previously described (Beenken et al. 2003) using FPR3757, its sarA mutant, and its sarA mutant carrying mutations in the indicated protease genes. Single asterisks indicate significance by comparison to the parent strain. Double asterisks indicate significance by comparison to the sarA mutant. As a control, biofilm formation was also assessed in LAC, its sarA mutant, and derivatives of thesarA mutant unable to produce aureolysin (Saur), unable to produce any extracellular protease (SP), or unable to produce any extracellular protease other than those encoded by the spl operon (SPspl+). Single asterisk indicates statistical significance by comparison to the sarA mutant. Double asterisks indicate significance by comparison to the Saur mutant.

Figure 1. R-Ras and RIN2 promote EC-to-ECM binding, adhesion, migration, and vascular morphogenesis; RIN2 mediates the pro-adhesive effects of R-Ras.

Figure 1. R-Ras and RIN2 promote EC-to-ECM binding, adhesion, migration, and vascular morphogenesis; RIN2 mediates the pro-adhesive effects of R-Ras.

Figure 1. R-Ras and RIN2 promote EC-to-ECM binding, adhesion, migration, and vascular morphogenesis; RIN2 mediates the pro-adhesive effects of R-Ras.

Figure 1. R-Ras and RIN2 promote EC-to-ECM binding, adhesion, migration, and vascular morphogenesis; RIN2 mediates the pro-adhesive effects of R-Ras.

Figure 1. R-Ras and RIN2 promote EC-to-ECM binding, adhesion, migration, and vascular morphogenesis; RIN2 mediates the pro-adhesive effects of R-Ras.

Figure 1. R-Ras and RIN2 promote EC-to-ECM binding, adhesion, migration, and vascular morphogenesis; RIN2 mediates the pro-adhesive effects of R-Ras.

Figure 1. R-Ras and RIN2 promote EC-to-ECM binding, adhesion, migration, and vascular morphogenesis; RIN2 mediates the pro-adhesive effects of R-Ras.

Figure 1. R-Ras and RIN2 promote EC-to-ECM binding, adhesion, migration, and vascular morphogenesis; RIN2 mediates the pro-adhesive effects of R-Ras.

Figure 6 shows the impact of mutating individual protease genes or operons in both the WT and sarA mutant as well as the derivatives of the sarA mutant in terms of biofilm formation.

Figure 3 shows the impact of mutating individual protease genes or operons in the WT and sarA mutant as well as the derivatives of the sarA mutant in terms of proteolytic activity.

Figure 9 shows the impact of purified aureolysin in contemporary clinical isolates as a function of methicillin resistance status. Methicillin is a member of the penicillin class.

Figure 10 shows the relative impact of aureolysin and dispersin B on biofilm formation.

Figure 8 shows the difference between biofilm formation in WT and sarA mutants.

Figure 7 shows the impact that mutating individual protease genes/operons in vivo has on the ability of WT and its isogenic sarA mutant to produce proteases. The repression of protease production in turn promotes biofilm formation.

Figure 6 shows the impact of mutating individual protease genes or operons in both the WT and sarA mutant in terms of biofilm formation.

Figure 5 shows the impact of purified extracellular proteases on dispersal of established biofilms.

Figure 3 shows the impact of mutating individual protease genes or operons in both the WT and sarA mutant in terms of proteolytic activity.

Figure 4 shows how purified extracellular proteases impact biofilm formation in LAC protease-deficient derivatives.

Figure 2 shows the impact of purified extracellular proteases aureolysin, SspA, ScpA, and SspB on biofilm formation.

Figure 1 defines the optimal conditions for biofilm formation in vitro for both WT and isogenic sarA mutants.

Figure 1 shows that the left panel shows the entire complex, whereas the right panel shows a zoomed image of the cephalosporin binding pocket. The Staphylococcus aureus strain depicted in the crystal structure (PDB 3HUM) [30], Col, is the parental strain of the Colnex strain used in the current study (Table 1). Mutant residues in PBP4 identified by selection with ceftaroline or ceftobiprole are highlighted in blue. The ligand marked in yellow is cefotaxime.

figure A. shows Vancomycin minimum inhibitory concentrations (MICs) were determined by Etest for A5937, A5937Δstp1, the complemented strain A5937Δstp1-C, and the vancomycin nonsusceptible isolate A5940. Values in parentheses represent MICs based on broth dilution.Figure B. shows Determination of vancomycin heteroresistance was performed using population analysis profiling. The stp1 deletion mutant had subpopulations that grew in the nonsusceptible range (>2 µg/mL); this was not seen in the parent strain (A5937) but was more pronounced in the clinical vancomycin-intermediate S. aureus daughter strain (A5940). CFU, colony-forming unit. Figure C. shows transmission electron microscopy was performed to determine cell wall thickness. Three representative cells from each strain are shown, and values represent mean cell wall thickness (95% confidence interval).

Table 1. Distribution of various virulence, regulatory and toxin genes.