Fig. 3: Development of v3b PE-eVLPs, which use an alternative PE recruitment mechanism. | Nature Biotechnology

Fig. 3: Development of v3b PE-eVLPs, which use an alternative PE recruitment mechanism.

From: Engineered virus-like particles for transient delivery of prime editor ribonucleoprotein complexes in vivo

Fig. 3

a, Schematic of coiled-coil peptide-dependent recruitment of PE. NES, nuclear export signal. NLS, nuclear localization signal. b, Comparison of prime editing efficiency with v2.3 PE-eVLPs versus the alternative system employing coiled-coil peptide for the recruitment of PE. c, Schematic of v3b PE-eVLP system. NES, nuclear export signal. NLS, nuclear localization signal. d, Heatmap of editing efficiencies from stoichiometry optimization of Gag–Pol, Gag–COM–Pol and Gag–P3–Pol plasmids for production of v3b PE-eVLPs. e, Prime editing efficiencies comparing v1.1 PE2-eVLPs, v3 PE3-eVLPs and v3b PE3-eVLPs at Dnmt1, FANCF, Col12a1 and HEK3 locus in N2A and HEK293T cells. f, Comparison of editing efficiencies for four different prime edits targeting HEK4 locus in HEK293T cells following plasmid transfection or treatment with v3b PE-eVLPs at the on-target HEK4 site and known off-target sites for the corresponding pegRNA1. Values shown in all graphs and heatmaps represent the average prime editing efficiency of three biological replicates, and error bars represent the standard deviation. Data were fitted to four-parameter logistic curves using nonlinear regression. For all conditions other than f, 30,000–35,000 cells were treated with eVLPs containing ~2.5 × 108 eVLPs μl−1.

Back to article page