The Bacterial Defensin Resistance Protein MprF Consists of Separable Domains for Lipid Lysinylation and Antimicrobial Peptide Repulsion
Figure 5
Impact of the hydrophobic N-terminal domain of MprF on the ability of Lys-PG to repulse cationic cytochrome c and to reach the outer leaflet of the cytoplasmic membrane.
A) The capacities of S. aureus wild-type (WT) and ΔmprF (left panel) or ΔmprF containing the indicated plasmids (right panel) to bind cytochrome c were compared. B) Inner and outer-leaflet localization of Lys-PG in ΔmprF bearing the indicated plasmids was determined by analyzing the ability of the membrane-impermeable fluorescent dye fluorescamine to react with Lys-PG. pRB474 and pTX16 are empty control plasmids. Means and SEM of three (A) and four to eight replicas from two (B) independent experiments are shown. *, P<0.05; **, P<0.01; ns, not significantly different versus S. aureus WT (A, left panel) or ΔmprF containing plasmids pRB474mprF and pTX16 (A, right panel).