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. 2009 Dec 4;5(12):e1000685. doi: 10.1371/journal.ppat.1000685

Figure 1. Lytic activities of apoL1.

Figure 1

A. Schematic representation of apoL1 and apoL1 variants analyzed in this work, with indication of the amino acid residues delineating the three protein domains (see ref. 4 for details). B. Colicin-like activity of WT and mutant apoL1. pCDF-DUET plasmids encoding apoL1 variants provided with a C-terminal V5-His6 tag were transfected into E. coli BL21(DE3). In the case of the deletion (del) variants, an N-terminal bacterial signal peptide (pelB) was added. After overnight incubation at 37°C the bacterial plating efficiency was scored comparing expression induction by IPTG addition or non-induction by glucose (Glc) addition, or comparing the effect of pH. The ΔH9–H10 apoL1 mutant lacks the region encoding helices 9 and 10 of the pore-forming domain. C. Trypanolytic potential of various apoL1 variants, as determined on T. b. brucei after 24 h–incubation in vitro (ctrl = control without apoL1).